The Ghanaian Pig Mask of Tribal Trends

5 August 2022

by Eben van Tonder


The pig is one of the most iconic domesticated animals with a rich history. I have a special interest in heritage breeds. Such a breed was powerfully introduced to me today when I visited the African indigenous art dealer, Tribal Trends in the city bowl in Cape Town with the prolific entrepreneur from Nigeria, Haresh Keswani where we were hosted by the owner, Eugene Kramer and his wife, Miriam.

Tribal Trends, Winchester House, 72-74 Long St, Cape Town City Centre, Cape Town

While Haresh was looking for inspiration for one of his ventures, I was struck by a beautiful mask of a pig on the second story of one of their showrooms.

I am familiar with African masks featuring birds and other animals, but never a pig. How widely and from how early were pigs indigenous to Africa? Of course, the warthog and its related family are found across the continent, but a pig that resembles the Chinese pig was unusual. Eugene identified the mask as Ghanaian and while Haresh and he browsed through the multiple floors of exquisite artwork, I was on my phone googling indigenous pigs from Ghana.

(Giant) Forest Hog

My first suspect was the Giant Forst Hog. Was this the animal depicted in the mask?

The image was downloaded from Pinterest where the animal is described as “mostly nocturnal, & prefer the cover of the dense Congo rainforest to open savannah.” (Pinterest)

The giant forest hog, the only member of its genus, is native to wooded habitats in Africa and is generally considered the largest wild member of the pig family, Suidae; however, a few subspecies of the wild boar can reach an even larger size. Despite its large size and relatively wide distribution, it was first described only in 1904. (

The first photo I saw of the animal did not show the tusks and warts and the hair, prominently featured in the mask, made me wonder if what the artist tried to replicate in the mask was not the long hair. A closer examination showed that this is definitely not the animal represented in the mask.

Local West African Pigs – West African Dwarf pig (Nigeria) and Ashanti pig (Ghana)

A Review in the Journal of Advanced Veterinary Research (Volume 10, Issue 1, 2020), elucidated the animal celebrated by the mask as the local West African pig.

Local West African pig boar.

Evaluating the long snout and the ears makes the identity unmistakable!

These pigs are found in West Africa, from Senegal to Nigeria (Meyer, 2019) “This breed origin is controversial, but recent work on molecular genetic characterization has admitted that local pigs’ breeds could come from the Middle East through Egypt and from the Far-East through trades across the Indian Ocean, this because alleles and genes of breeds from these areas are found in local breeds (Ramírez et al., 2009; Amills et al., 2013; Lesur-Gebremariam, 2014; Agbokounou et al., 2016; Osei-Amponsah et al., 2017). (Dotche, 2020)

Several terminologies are used to name this animal according to country. For example, it is called West African Dwarf pig (Nigeria) and Ashanti pig (Ghana) (Meyer, 2019). This breed has almost the same phenotypic characteristics in all African countries where it exists. It is a small animal that has a uniform black or white colour, sometimes piebald, and with long or short dense hairs (Alenyorege et al., 2015; Youssao et al., 2018). Its body is 49 to 52 cm long and ends with a long head (25 cm) (Okoro et al., 2015; Youssao et al., 2018). Found in most African countries, it tolerates food irregularities and is heat-resistant, and for that is more bred in traditional livestock farms, especially in rural areas (Agbokounou et al., 2016; Dotché et al., 2018). (Dotche, 2020)

In this system, the breeder gives little importance to his feeding and to health monitoring. The feeding consists of the distribution of cereal and fruit residues, leguminous plants and food leftovers (Ossebi et al., 2018). It is appreciated by breeders for its disease resistance and by consumers for its meat quality (Agbokounou et al., 2016). Unfortunately, these performances are low and are improved by exotic pigs in farms. The weight at 180 days old is 19.2 kg (Darfour-Oduro et al., 2009) and when the animal is 365 days old (1 year) (Abdul-Rahman et al., 2016), its weight is 51 kg. Beyond one year, the weight reaches 62 kg (Karnuah et al., 2018). (Dotche, 2020)

They are reared mostly by small rural farmers in a traditional system. Their meat is highly valued by consumers compared to exotic pork because it is marbled (Deka, 2008).” It is preferred over exotic breeds such as the Large White, Landrace, Pietrain, or the Meishan. (Dotche, 2020)

Masks and Africa

We identified the pig represented in the mask, but what is the significance of maskes in Africa? Afomia Tesfaye writes that “African masks are greatly appreciated for their artistic value. They adorn the walls of some of the most recognized museums and galleries across the world. Many of us incorporate masks into our homes to add an exotic flair to our décor, but it is important to recognize that beneath their surface beauty, these mysterious faces possess a deeper significance. Understanding their history is an essential part of appreciating their cultural, symbolic, and aesthetic value.” (Tesfaye)

“The existence of African masks can be traced as far back as the Stone Age. For thousands of years, African people have incorporated tribal masks into their cultural ceremonies, rituals, and celebrations. Each of these creations is designed according to the particular traditions of their region. Designs vary from modest and plain to highly elaborate in appearance.” (Tesfaye)

“African villagers hold deep and complex beliefs around masking ceremonies. It is thought that when a person (often a man) wears a mask, he becomes a sort of medium, capable of communicating with spirits and ancestors on behalf of the community. This is an effort to control the forces of good and evil by calling on the intervention and blessings of spirits to support and guide the community through such crucial life events as war preparation, crop harvesting, marriage, fertility, and burials.” (Tesfaye)

“Since masks function as a vessel for contact with various spirit powers, the creator of the mask must possess both the technical skill and spiritual knowledge required to make them. These talented artisans. . . sculpt faces in the shape of perfectly symmetrical human or animal forms using such varied materials as pottery, textiles, copper, and aluminium. It is believed that these artisans are able to sense the “spirit power” that dwells in the materials they use to create their pieces. The energy of the spirit is thought to inhabit the artists’ instruments, so their tools must be handled with extreme caution. As the mask gradually begins to take shape, the object is believed to acquire more supernatural abilities. In some cultures, it is thought that this intimate relationship between the maker and his creation enables the artist himself to absorb some of its magic power. or bronze. They finalize their creations by embellishing them with such varied materials as clay, ivory, horn, stone, feathers, and straw. Sometimes masks are made in the image of a female face which would be typically based on a particular culture’s ideal of feminine beauty.” (Tesfaye)

“Mask-wearing has always been a vital part of African life. Masks are worn to disguise the face, sometimes in conjunction with a costume that covers the entire body. Their purpose is to enable the wearer to transform himself into the entity depicted by the mask. In essence, the wearer works in tandem with the mask during a ceremony to release its hidden power.” (Tesfaye)

“While spectators from the community observe, the wearer (again, often a man,) engages in a highly animated performance in which he goes into a deep trance until the spirit completely inhabits and possesses his body. Music (primarily drums,) dance, song, and prayer are used to induce a state of trance by which this transformation can occur. This sets the stage for a supernatural exchange between the dancer and spirits, ancestors and other entities.” (Tesfaye)

“In contemporary Africa, masks are no longer as commonly used for tribal ceremonies though they still represent one of the continent’s most vibrant contributions to the arts. The rich and vast offering of masks on the NOVICA site celebrates and honours the heritage of African masks and the talented artisans that create them.” (Tesfaye)


It is of significance that it is the local West African pig that is celebrated in the mask exhibited by Tribal Trends in Cape Town, reflecting on a tradition we know existed at least in Ghana which celebrates these remarkable animals. What was it that the artist saw in these pigs that inspired him to create the mask? Certainly, the tradition of using these animals for inspiration must be ancient! Haresh said it well today that art is not mind. Art is spirit! The mesmerising influence of these remarkable animals on me can not be explained by rational thought and like art itself, the connection is spirit and soul!


Ignace O. Dotche, Gabriel A. Bonou, Mahamadou Dahouda, Nicolas Antoine-Moussiaux, Jean-Paul Dehoux, Guy Apollinaire Mensah, Souaïbou Farougou, Pierre Thilmant, Issaka Youssao Abdou Karim, Benoît G. Koutinhouin.(2020) Reproductive Performances of Local Pigs in West African Countries: A Review. Journal of Advanced Veterinary Research, Volume 10, Issue 1, 2020, Pages: 49-55, (ISSN: 2090-6277/2090-6269/ © 2011-2020 JAVR),

All other references are linked in the text to the source.

Ancient Plant Curing of Meats

Ancient plant Curing of Meats
Eben van Tonder
15 February 2022


I have been studying the history of meat curing and ham/ bacon processing for well over 15 years. Over the years I looked at the use of saltpetre and the older curing salt from antiquity, sal ammoniac. I considered long term salt curing. I searched the world for natural nitrite and sal ammoniac deposits and scratched around in remote parts of the globe for signs of an ancient meat curing culture.

You see, the food we eat is not always the thing that make the headlines or what historians love writing about. Yet, the precise nature of recipes and the uninterrupted mother to children transmission of culinary history, the way that the food we grew up with sticks and transmits our culture and becomes as important to us as our language makes food and recipes one of our best glimpses into the past, even to a time when writing did not exist or was not universally known.

I started to suspect that nitrate curing of meat from plant matter played just as important role in establishing meat curing as nitrate and ammonia salts. The subject was so vast and so many clues came to me from so many angles over so many years that I was uncertain where to start the story. The task was daunting!

In Lagos, I met Doğan Genç and Ayhan Yilmaz from Turkey on a business trip from the ancient city of Bursa, on behalf of their refrigeration company, Kaplanar. Unknown to them, the one morning they spent with me in a small boardroom at Spar Head Office in Nigeria would be the event that gave me the courage to dive into the subject. They introduced me to an ancient Turkish dish, Pastrma or Salt Cured Beef. It has a rich and relevant history. It became the point where I take a deep breath and launch into the subject of the ancient origins of the plant curing of meat! Let’s begin the story by looking at the history of Pastrima and immediately branching out to the general geographical and important region of the Black Sea and another famous method of curing meat, namely with horse sweat!

History of Pastırma

Pastirma from THE HISTORY OF BASTA by Mustafa CINGIL

“The nomad Turks of Central Asia has developed many methods to preserve their surplus food. Some of these methods and the foodstuff discovered based on these methods have survived until the current times. “Pastırma” the salt-cured, air-dried beef is one of these foodstuffs that is inherited from the Central Asian Turks.” (TFC)

Cingil (2019) reports that the Turks used an area’s suitability for drying meat as a criterion for settlement. They would hang meat in a tree and observe how long it takes to dry or if it decays. If it remains in good condition for a long time, they will settle there. It is reported that Emir Timur selected Samarkand using this method.

“The Turkic tribes, who lived in the steps of Central Asia, before 11th Century A.D., have salted and air-dried their leftover meats to preserve it. Due to their nomadic nature, the dried meat was stored in leather bags and consumed, as necessary.” Weber Baldamus, in his world history book, mentions an unusual method of treating meat, based on the information obtained from Amiadus of Antioch” or Amiadus of Antakya who lived between 273-375. He writes, “Hun Turks eat dried meat and the meat that they crushed between the horse’s saddle and calf, along with fresh game animals, together with various herbs.” (Cingil, 2019) According to Cingil (2019), this is also the earliest reference to pastirma.

Jean, sire de Joinville, the great chronicler of medieval France who wrote in the 1200s, mentions “steak tartare” as “a Mongol culinary technique of placing the steak between the saddle and the saddle blanket, and eaten raw once all the blood has been beaten out.” (Turnbull, 2003) This is a famous Western reference and one that people love to use to show that de Joinville probably got the report wrong, but after a thorough investigation of the matter I believe the critics got it wrong and not de Joinville.

TFC is one of the authors who dispute the factualness of these claims. He contends that “the Huns actually stored the meats in the pockets found on the saddles. Therefore, the meat never touched the body of the horse.” He refers to the old sources of the Huns as per the Hungarian National Museum. (TFC) I see no contradiction between these sources. The meat could have been stored in the saddlebags as per the Hungarian National Museum and some riders may have chosen to place them between the saddle cloth and the saddle as described by both Jea, sire de Joinville and Amiadus. The next reference comes to us in the 1600s.

Władysław Łoś, responded to a question about placing the meat between the saddle cloth and the saddle in an online forum by pointing out that the story was again popularised in the 17th century, “by a certain Guillaume Le Vasseur de Beauplan, a French military engineer in service of Poland, author of the book “Description des contrés du Royaume de Pologne” (“Description of the countries of the Polish Kingdom”). He repeated the Joinvilles story but this time his reference is to contemporaneous Tatar horsemen in the service of the Polish military.” He points out that the Tatars in question were not Mongols, but a Turkish tribe.

That this experience repeated itself in other parts of the world during different times is clear from history. Using the sweat of horses to cure meat, intentionally or unintentionally was practised by the Boers in South Africa. I refer to this in my article, Saltpeter, Horse Sweat, and Biltong where I explore the chemistry of sweat and the reaction with the meat and refer to the word we use on South African farms to this day in reference to the white sweat of horses as “saltpetre,” the enigmatic salt of antiquity used to cure meat and as a key ingredient in gunpowder. Saltpetre is potassium nitrate, today used in long term curing.

Ancient Meat Preservation

When one talks about ancient culinary processes, it is important to understand that the human view of bodily excretions in antiquity was vastly different from the current views. Anything generated by the body, including animals, was viewed as very special and endowed with powers, useful for humans. I refer to my article, How did Ancient Humans Preserve Food? Levine (1999), in her work on the origins of horse domestication, presented “some results from an ongoing ethnoarchaeological study of equine pastoralism on the Eurasian steppe. The data have arisen principally in the course of five interviews, conducted between 1989 and 1992, with people involved with horse husbandry in Mongolia and northern Kazakhstan in the recent past or present.”

She writes that “The horse is used extensively in Kazakh folk medicine (Toktabaev 1992). Horse fat, excrement, bone, hair, liver, kidney, and stomach are used in the treatment of many ailments. . . Back problems were treated by wrapping the sufferer in a fresh horse skin.” Importantly for our study, she says that horse sweat had a very specific medicinal value. “Horse sweat is said to cure gastric diseases, ulcers, typhoid fever, plague, fever, and cancer of the gullet.” The medicinal usages probably followed the discovery of its effect on the meat and the subsequent ingestion of it. Levine, writing on the general usefulness of the horse makes the same point about sweat again when she writes, “The horse can move rapidly and easily long distances over hard ground, providing its owners with both mobility (riding, packing, traction) and nourishment (milk, meat, fat). Other products, such as bone, hoof, hair, hide, excrement, and even sweat, are also valued, for example, as fuel, raw materials for the fabrication of tools, utensils, musical instruments, and other objects, and for medicinal purposes.”

The point is that using sweat to cure meat is not farfetched. I had a suspicion for a long time that urine and sweat had both been used in antiquity in meat preservation and from food, it entered medicinal use and gained religious value. The only way that meat can be cured is through access to nitrate or nitrite. It required nitrogen. Reduction takes place through bacteria from nitrates to nitrites and chemically from nitrites to nitric oxide which is the species responsible for linking up with the hem moiety on the meat protein and which then produces the cured colour of cured meat. The controlling mechanism of the entire process is one of reduction.

The only other way it can happen is through the oxidation of l-arginine by nitric oxide synthase. This requires time and the right conditions as far as temperature is concerned and metabolic water as we see in long term dry ageing of hams and bacon. Where reduction is easily managed, isolating, and harvesting oxidation enzymes are prohibitively expensive. The only way it can be done economically is through time and using what is already in the muscle. There should be no doubt in anybody’s mind that the basic curing reaction of accessing one nitrogen atom and one oxygen atom to form NO is the basis of curing. Without it, curing is not possible and what you have at best is salted meat.

Medical, Culinary, Religious and Military Value of Nitrogen

Nitrogen was accessed for medical, culinary, religious and military uses from antiquity through Saltpeter (nitrate salts). I have written extensively about this and refers you to Nitrate salt’s epic journey: From Turfan in China, through Nepal to North India.

My initial focus was on nitrate salts found in desert areas and in certain caves. I discovered the two curing salts of choice for ancient people as ammonium nitrate (sal ammoniac) (The Sal Ammoniac Project) and the various nitrate salts. Later, humans mastered the art of producing saltpetre as it became important in the ancient worlds arms race with its key role in gunpowder.

Ray, talking about the arrival of saltpetre production technology in India, says that “the manufacture of nitre was. . . most probably introduced into India after the adoption of gunpowder as an implement of war.”  (Ray, P. C., 1902: 99 – 100)  According to Frey, the watershed time for India between the age of the blade and the age of the gun came in the early sixteenth century.

The area of the world where we are focussing on Turkey to the south of the Black Sea and across the Caucuses mountains into modern-day Russia and Mongolia yields ample historical record of the importance of these salts. Frey states that “it is likely that Mongols who introduced the making of fireworks to India in the mid-thirteenth century. We know almost nothing about saltpetre production during this early period, but technical expertise apparently diffused with the adoption of rocketry and eventually artillery by Indian rulers in the fourteenth century. The break-up of the Delhi Sultanate, the rise of regional states, and the growing presence of Turkish mercenaries in India may be linked to the establishment of regular saltpetre production and the adoption and use of gunpowder weapons.”  (Frey, J. W.; 2009: 512)

It speaks to the sophistication of Mongal and Turkish technology related to nitrate production.  In Arabic, saltpetre (nitrate salt) was referred to as Chinese snow, for, according to Needham, it was recognised and used in China long before anywhere else. “The oldest extant Arabic mention is in the Kitiib al-Jiimi’ fi al-Adwiya al-Mufrilda (Book of the Assembly of Medical Simples) finished by Abti Muhammad al-Mllaqi Ibn al-Baitarg about 1240 AD. Others follow shortly after.  (Needham, J.. 1980:  193, 194)

The use of saltpetre (nitrate salts) in meat curing grew hand in hand with the availability of saltpetre in a region. At first nitrate deposits were limited to desert areas and certain caves. One of the earliest examples of this is the Turfan depression due to the enormous natural nitrate deposits that are found on the top layer of the soil. Refer to Salt – 7000 years of meat-curing, Nitrate Salts Epic Journey:  From Turfan in China, through Nepal to North India and And then the mummies spoke!

As my investigations into the ancient origins of meat curing continued, I discovered the link between sea travel and nitrite curing. Sea travel is a great example of an activity that necessitated storing food for a long time. In keeping with the ancient practice of storing meat in water, they most probably used seawater. Dr Francois Mellett, a renowned South African meat scientist, shared a theory with me related to the curing of meat stored in seawater. He writes, “I have a theory that curing started even earlier by early seafarers: when a protein is placed in seawater, the surface amino acids are de-aminated to form nitrite for a period of 4 to 6 weeks. Nitrite is then converted to nitrate over the next 4 weeks. Finally, ammonia and ammonia are formed from nitrate. It is possible that they preserved meat in seawater barrels and that the whole process of curing was discovered accidentally.” I applied Mellett’s logic to coastal communities when I discovered the importance of meat storage in seawater by ancient coastal settlements and small groups migrating along the coastal regions of the world.

Of course, I saw horse domestication as another event, which, like seafaring, would necessitate the long term storage of meat.

Linking Meat Curing with Horse Domestication

I have known that curing would be intimately associated with the domestication of horses for a long time. I started to research the people who lived in the region where horses were domesticated. I looked at the Scythians (Research Notes on the Scythians). Horse domestication I dealt with in The Turfan Depression links with the Black Sea Region.

East of the Dnieper River within the Don and Volga basins, on the Western Front of what later would be occupied by the Scythians, between 4600 and 4200 years ago, a dominant genetic horse population appeared which replaced the wild horses that roamed Eurasia for millennia.

No sooner did I discover this, and I found myself delving through old records about the Caucasus, or Caucasia, a region spanning Europe and Asia to understand the nature of their nitrate (saltpetre) deposits. Why? Because it is linked with the origins of the art of meat curing which I suspect happened in this region and to the north of it which again is linked to Turfan, the area I first suspected as the site where meat curing became an art, but the lack of solid evidence of a long meat curing tradition from old records from the Turfan area made me suspect that they only used it at a major source for Saltpeter and Sal Ammoniac, the primary two curing salts from antiquity. These were traded along the silk road that ran into Europe. The creation of a meat curing tradition happened somewhere else.

Why the link between the Caucasus and meat curing? Because my suspicion is that meat curing was transformed into an art (practices on large scale according to set principles and procedures) in an area where the horse was domesticated because no other event would have given rise more to the need for this than the domestication of the horse (other than sea voyages). As the exploration of vast distances and military exploits became possible, following horse domestication, the need would have existed to carry food along on these campaigns and since we know the Scythians were more than likely involved in the domestication of the horse (or the ancestors of what became the Scythian people), we know that animal protein (dairy and meat) was a major part of their diet.

> The Caucasus

I begin my investigation at the southern edge of the area where horse domestication took place.

Archaeological and geological records from the Caucasus are very sparse, to say the least, but it is the one region, adjacent to the site of horse domestication natural nitrate deposits occur. From there my interest in it. Well, my interest is in the entire Don and Volga basins regions (mostly, present-day Russia) between 2000 BCE and 2200 BCE. I begin in the south and will work my way north.

So, what am I looking for in the Caucasus mountains? Saltpetre and any other clue to develop the ancient picture for me.

I came across this fascinating book by McCulloch, John Ramsy. (1845) M’Culloch’s Universal Gazetteer: A Dictionary, Geographical, Statistical, and Historical, of the Various Countries, Places, and Principal Natural Objects in the World.

> Minerals

About minerals found in the Caucus mountains, McCulloch writes, “Iron, Copper, Saltpetre, sulfur, and lead are found, the last in tolerable large quantities. Salt is almost wholly wanting.” So, a little bit of saltpetre, which explains importing it from Turfan. No salt – very interesting! It was plentiful in the Don and Volga basins. . . more on this later!

> Vegetation

I add a section of what I will be looking for in the Don and Volga basins region namely vegetables. About this McCulloch writes: “In amount and variety of vegetation the Caucasian regions seem to be unrivalled. Chardin, writing in 1692, says, ‘Mount Caucasus, till ye come to the very top of it is extremely fruitful,’ and Spencer in 1838 says, ‘However high the ascent, we see luxuriant vegetation mingling even with the snow of centuries.’ Nearly every tree, shrub, fruit, grain, and flower found from the limit of the temperature zone to the pole is native to or may be raised in the Caucuses. The Northern bases consist of arable land of excellent quality, meadows of the finest grass and dwarf wood in great abundance.” He continues to describe the quality of the soul in the regions to the south, east and west in equal lofty terms.

> Fruits, Vegetables, Grains

He continues, “Among the standard fruits are found the date palm, the jujube, quince, cherry, olive, wild apricot and willow leaved pear. Pomegranates, figs, and mulberries grow wild in all the warmer valleys and vines twine around the standard trees to a very great elevation up the mountains. . . . In addition to the vine, the other climbing plants are innumerable, which, mixing with the standards, the bramble fruits (raspberries, blackberries &c,) and other dwarf woods form a density of vegetation which is impossible to penetrate, unless a passage be hewn with the hatchet. Rye, barley, oats, wheat, millet are abundantly raised, even as high as 7500 ft. above the sea, and besides these grains, the warmer plains and valleys produce flowers of every scent and dye, cotton, rice, flax, hemp, tobacco, and indigo, with every variety of cucumber and melon.”

McCulloch quotes several texts to prove that the list just given is only a small sample of what is available from these regions, in particular from Georgia.

The list given is extremely important because it feeds into something I’ve picked up from the geological record of the territory occupied by the Scythians, especially the region where horse domestication took place in other research. A picture is forming that may alter our traditional view of the trajectory of the art of meat curing dramatically but patience is called for. Lots of investigation must be done across vast regions before I can venture to put the final picture together. If what I suspect happened is true, it will be truly revolutionary, but let the data form the picture.

The one sentence that caught my eye will follow. It’s under his treatment of the animals which are as innumerable as the plants. The detail is not as important as the list of plants and I understand that his lists of plants go back probably to the earliest, to the 1600s. It does not give us a list of what was there in 2000 BCE, but we will get there. The picture is, however, that most mentioned here were indigenous to the area and grew wild.

> Cattle

The first important comment relates to cattle. He writes, “This is also home of wild cattle; the large species (the Aurochs) being found in the forests; while of the domesticated kinds, the varieties are numerous and serviceable.” I wish I could have seen the aurochs!

> Horses

This is the actual point I want to make here following on the identification of the exact location where horse domestication took place through DNA research. He writes the following of the horse which we know has been domesticated in the region directly adjacent and to the north!”The horses of the Caucasus have been famous from very high antiquity, the Bechtag mountains having been formerly called Hippicon (ἱππικόν) from the number of these animals which were grazed upon its side (Ptolemy, v., 9). They are not less numerous in the present day and are among the very finest varieties of the species.”

These horses were indeed famed throughout the ancient world, and it stands to reason that he is describing none other the descendants of the earliest domesticated horses, referring to their excellence based on the superior qualities they had for the horseman. In other words, domesticated horses but further refined through selective breeding.

I find it absolutely fascinating that what DNA research in 2021established could have been accurately predicted based on a careful reading of these old texts. That the region had superior technology related to horse husbandry and breeding cannot be disputed and I am sure that the process which started domestication did not stop. They continued their selective breeding, no doubt! The technology that brought the events about in the 2000s BCE kept producing superior animals and it is fascinating that the traditions continued from 2000 BCE into the 1800s A.D.. It is therefore not far-fetched at all to expect meat curing to be still practised at a superior level in regions where it originated. Of course, I can imagine events that could wipe such traditions out, but as a very broad general rule of thumb, I can see how a deeper understanding of curing in a region would point to an older tradition.

> The Nations of the Caucuses

There is probably no other part of the world, except Africa, S. of the Sahara, where so many nations and languages are collected within so small a space as in the Caucasus. Guldenstadt gives a list of seven different nations, besides Tartars, who speak languages radically different, and who are again subdivided into almost innumerable tribes, among whom the varieties of dialect are nearly infinite. The principal nations he thus enumerates

1. Georgians;

2. Basians;

3. Abchasians;

4. Tcherkessians;

5. Oketiens;

6. Kistiens;

7. Lesghians;

8. Tartars.

(Reise, i., 458 – 495.)

Of these the most numerous and important are the Georgians and Circassians or Tcherkessians; but the Abchasians and Okesians, called by Pallas and Klaproth Abassians and Osetians, are also powerful tribes. In habits and manners, a strong resemblance is observed among them all; they are usually wandering hunters and warriors, for which occupations their country is peculiarly fitted, and only in inferior degree shepherds or agriculturists. A partial exception must, however, be made to this general character in favour of the Georgians, who reside in towns, and have long possessed a fixed form of government and internal polity; but for the rest, they appear to possess the erratic disposition, reckless courage, boundless hospitality, and much of the predatory habits which mark the Arab and other half barbarous people. (See CIRCASSIA, GEORGIA, &c.) It is well known that Blumenbach looked here for the origin of his first and most intellectual race of men (the Caucasian); but for this, as already stated (anté 177). there is not a particle of evidence historical or philological. The Caucasians though surrounded by the means of improvement, and occupy a country more favourably situated than that of Switzerland, have made no progress either in arts or arms; and continue to this day the same unlettered barbarians as in the day of Herodotus. (Clio, 203.) They have fine physical forms, but their mental endowments are of the most inferior description.”

Next, he describes the nations living in these regions and their technology related to warfare.

Meat Preservation with Fruits and Vegetables

I found that all the nations around the Black Sea have long and ancient meat curing traditions. Georgie, Azerbaijan, Moldovia, Romania, Bulgaria, and of course, Turkey. In fact, we began with Doğan Genç and Ayhan Yilmaz from Kaplanar visiting Lagos and alerting me to the existence of Pastirma. Unknowing to them, it would provide the crucial link I long suspected that ancients not only cured their meat with the sweat of horses and nitrate and sal ammonia salts from desert regions but more importantly with plants!

It is, therefore, from Turkey that the rest of the story comes. The traditions of curing meat with plant matter are generally from Central Asia. The dish that unlocked the plant-based curing techniques for me is partirma.

TFC writes that “the oldest meat preservation method is to salt and air-dry the meat in the sun. Different cultures of the world have different meat preservation methods. The method used to make “pastırma” is invented by the Central Asian Turks, and it is the forerunner of today’s “pastırma”, a term which literally means ‘being pressed’ in Turkish.” (TFC)

“Looking into the old scripts, such as “Divan-ü Lügat-it Türk”, the first Turkish- Arabic dictionary written by Mahmoud al-Kashgari, the word “pastırma” was not used. Instead “basturmak” was used, which means to place something under a very heavy object. In the Turkish language used by the Central Asian Turks, there were other words such as “kedhirilmek” or “kakaç” used which means dried meat, and the word “kak” was used for everything dried.” (TFC)

“Based on the information from “Divan-ü Lügat-it Türk,” during autumn, meat would be mixed with some spices, dried and stored until spring. During spring the animals would lose weight and their meat becomes flavorless. Therefore, those who have stored up some “pastırma” would have access to good tasty meat.” (TFC)

Anatolia, also known as Asia Minor, is a large peninsula in Western Asia and the westernmost protrusion of the Asian continent. It constitutes a major part of modern-day Turkey. “Arrival of “pastırma” in Anatolia was especially well received in the city of Kayseri. The 17th-century Turkish traveller Evliya Çelebi, praised “pastırma” of Kayseri in his Book of Travels, and Kayseri “pastırma” is still regarded as the finest of all. Although there are several other cities that are known to make “pastırma,” Kayseri is the only one that is associated with this delicacy. Due to the fact that it is an important trade that passes from generation to generation, the climate of Kayseri and the high amounts of nitrate found in the city water also plays a very important role in this matter.” (TFC)

“Good quality “pastırma” is a delicacy with a wonderful flavor. Although “pastırma” can also be made with mutton or goat’s meat, beef is preferred. During the Ottoman period, although they almost always consumed lamb in their dishes, when making “pastırma” beef was the meat of choice.” (TFC) 

Making of Pastırma

“Cattle, mainly from the eastern province of Kars, are brought to Kayseri, where they are slaughtered, and the meat made into “pastırma” at factories found on the northwest of the city. The different cuts of meat produce different types of “pastırma.” There are 19 to 26 varieties depending on the size of the animal. Extra fine qualities are those made from tenderloin and loin; fine qualities are made from cuts like the shank, leg, tranche and shoulder; and low quality from the leg, brisket, flank, neck and similar cuts. The many tons of “pastırma” produced in Kayseri are almost all sold for domestic consumption all over Turkey.” (TFC)

“The ideal season for making “pastırma” in autumn. The season starts by mid-September and continues until the end of autumn. This weather presents qualities such as; sunny and clear skies, low humidity and mild wind that are ideal conditions for drying and maturing.  The “pastırma” making process consists of 5 stages that are; procurement of the animals, preparation of the meat, processing of meat, coating and packaging.” (TFC)

“The making of “pastırma” lasts for about a month. The freshly slaughtered meat rests at room temperature for 4-8 hours before being cut into pieces suitable for making “pastırma.” The meat is slashed and salted on one side, stacked, and left for 24 hours to rest. The same process is done to the other side. After the second 24 hour period, meat slabs are rinsed with plenty of water to remove the excess salt, and left to dry outdoors for a period varying between 3 to 10 days, depending on the weather. After some further processing, the meat is hung up to dry again, this time in the shade and spaced out so that they do not touch one another. After 3 to 6 days, they are covered with a paste known as “çemen” paste.  “Çemen” is composed of fenugreek seed flour, garlic and powdered red chilli pepper and water to form a paste. This paste covering the slabs of “pastırma” plays an important role in the flavour, and protects the meat from drying and spoiling by cutting its contact with air. The excess “çemen” is removed, leaving a thin layer, and left to dry again. Finally “pastırma” is ready for consumption.” (TFC)

“When buying “pastırma”, make sure that it has a bright red hue, and cut very thinly with a cleaver. “Pastırma” can be consumed freshly on its own, or cooked with eggs, tomatoes, inside the white bean stew or “börek” (the savoury pastry). In the Anatolian region of Turkey it is also added to bulghur rice pilaf and sometimes in stuffed grape leaves.” (TFC)

“In conclusion “pastırma” is an important culinary legacy from the Turkish forefathers and a delicious delicacy that adds a depth of flavour to any type of food it’s combined with.” (TFC)

An insightful video on how to make Pastirma.


Pastrma became my entry point into the ancient art of curing met with plant matter replete with nitrates. Over the months to come I will delve into the wonderful technical and scientific considerations which are brought up by the subject. In our time, fermentation of brine produced from plant matter with starter culture bacteria to affect the conversion of nitrates to nitrites and the chemical and enzymatic creation of Nitric Oxide which is responsible for meat curing became a trend as a way to sidestep the legislative requirement to declare the direct use of sodium nitrate or nitrite in meat cures. What I discovered is that this is nothing new. It stands in an ancient tradition of recognised curing systems. In our technical evaluation of the method, we will discover the vast accumulation of health benefits that accrue to products cured in this way. I am escited to begin this facinating yourney with you!

More History of Pastirma by Mustafa CINGIL

It is mentioned in the documents that it was among the unique products of the Ottoman Palace Cuisine (matbah-ı amire) in the 1500s and that it was among the favourite foods of the cuisine with the name “Pastama-ı Kayseriyye”.

Again, in the Seciye Registers of the Ottoman Period Ankara Province (1591-1592), it was complained that the pastrami sent every year did not come from Kayseri.

The famous traveler Evliyâ Çelebi, after describing the white bread, lavash pastry and layered pastry when he came to Kayseri when he came to Kayseri, in his Travels, said, “There is no cumin bacon and musk-cented broth, which are known as Lahim-i kadid (fat meat). He always goes to Istanbul as a gift”.

In 1880, British Lieutenant Ferdinand Bennet was describing the Kayseri Sanjak of Ankara province, the food habits of the region; Bulgur pilaf with meat, yoghurt, pita… He reported that more vegetables and fruits are eaten in summer, pastrami is consumed in winter, and 360,000 okkas of pastrami is exported from Kayseri to Istanbul in the same year.

The French traveler Vital Cuinet, who visited Anadalu in 1888-1890, described the commercial life of Kayseri and recorded that bacon, wool, carpets, animal skins, almonds and various fruits were exported from the city.

The first information about the production of pastrami is found in a Construction Book in 1869 and in Fahriye Hanım’s work titled “Housewife” written in 1894, and detailed information about Kayseri Pastrami is given.

German Ewald Banse, in his work on the observation and geography of Anatolia in 1919, wrote that “Germir Pastrami” is very famous while talking about Kayseri.

The first books on bacon and sausage production analysis in Turkey are in Ottoman Turkish; These are the books called “The Copy of Kayseri Pasdırmaları” (manufacturing style) and “Inspection of Pastrami and Sucuks of the Allelum (in general)”.

In the Ottoman period Kayseri Sanjak Yearbook, dated 1881-1891, it is stated that “Kayseri pastrami has gained a lot of fame.”

In one of his articles, the writer Mustafa Gümüşkaynak from Kayseri;

“Kayseri has neither cotton nor olives, nor tobacco, nor any natural product.
Nature has made it convenient to make only pastrami in this city.
When the season comes, the pastrami piri comes and sits on the summit of Erciyes.
Pastrami piri is strong like nature.
It makes winter summer, and summer turns into winter.
Pir enchants Kayseri.
Once enchanted, a bright summer comes to Kayseri.
The fat drips from the bacon.
This is called “Bacon Summer”.
Then it rains, and this is called “Bacon Rain”.
This precipitation destroys the dust.
Dusty bacon loses all its value.”

Kayseri is the homeland of fenugreek pastrami since the depths of history. The effect of its climate, nitrate water and traditional master-apprentice chain is great in this.

The weather is clear and sunny, low humidity and slightly windy in the autumn, when there is intense pastrami production in Kayseri. This environment allows the bacon to dry without getting wet, in the most correct and natural way.

As it can be seen, for years, “pastirma” is a very important part of Kayseri culture, about which poems, folk songs and epics have been written.

Of course, there will be bacon production in other cities.
But these never change the fact that “pastirma is from Kayseri”.
Just like Antep baklava,
Maraş ice cream…

In short…
-Pastirma and Ravioli both
belong to
Kayseri, they are from Kayseri!
It belongs to the people of Kayseri!
Just as;
-Like Sausage and Water Pastry!

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A website by the Turkish Cultural Foundation (TCF); Published under the section, Turkish Cuisine. Work reference “Her Yönüyle Pastırma”, Prof. Dr. O. Cenap Tekinşen, Doç Dr. Yusuf Doğruer, Selçuk Üniversitesi Basımevi, Konya 2000; Mustafa Çetinkaya / Skylife Magazine.


Frey, J. W..  2009.  The Indian Saltpeter Trade, the Military Revolution, and the Rise of Britain as a Global Superpower; from  The Historian, Vol. 71, No. 3 (FALL 2009), pp. 507-554;  Published by: Wiley Stable URL: Accessed: 23-09-2017 12:56 UTC

Levine, M. A.. (1999) Botai and the Origins of Horse Domestication. Journal of Anthropological Archaeology 18, 29–78 (1999) Article ID jaar.1998.0332, available online at http:/ /

McCulloch, John Ramsy. (1845) M’Culloch’s Universal Gazetteer: A Dictionary, Geographical, Statistical, and Historical, of the Various Countries, Places, and Principal Natural Objects in the World.

Needham, J.. 1959.  Science and Civilisation in China: Volume 3, Mathematics and the Sciences of the Heavens and the Earth.  Cambridge University Press.

Needham, J.. 1980.  Science and Civilisation in China: Volume 5, Chemical and Chemical Technology; Part IV:  SPAGYRICAL DISCOVERY AND INVENTION: APPARATUS, THEORIES AND GIFTS  Cambridge University Press.

Ray, P. C., 1902,  A History of Hindu Chemistry from the earliest time to the middle of the sixteenth century A.D..  Williams and Norgate.

Turnbull, S. (2003) Mongol Warriors, 1200 – 1350. Osprey Publishing

Władysław Łoś, studied Medieval Art & History at Warsaw University Poland (1985)

Cooldown of Products after Cooking

Cooldown of Products after Cooking
Eben van Tonder
17 February 2022


I am part of a team designing a meat processing factory in Lagos, Nigeria. I considered refrigeration from the standpoint of the effect of long term storage on product quality. In 2018 I did a comprehensive survey of The Freezing and Storage of Meat. I looked at weight loss during chilling and storage of meat. In 2019 I looked at Weight Loss During Chilling and Freezing of Meat. This time, the issue at hand is rapid cooling after cooking. Home Production of Quality Meats and Sausages by John Novak provided great introductory comments and he was kind enough to mail me the relevant chapter of his book.

He summarises the important point as follows: “Cooling down of cooked products is basically done to cross the danger zone (140o – 40oF; 60oC – 4oC) relatively fast. Cooked sausage at 160oF (72oC) so is still basically safe until the temperature drops down to about 60oC. Therefore, the restaurants are required to hold hot food at 140o F (60oC) or higher.” (Novak)

Regulatory Standard and Application

“The following standards come from the Food Safety and Inspection Service (FSIS), United States Department of Agriculture (USDA):

Compliance Guidelines for Cooling Heat-Treated Meat and Poultry Products (Stabilization)

It is very important that cooling be continuous through the given time/temperature control points. Excessive dwell time in the range of 130°F (55oC) to 80°F (27oC) is especially hazardous, as this is the range of most rapid growth for the clostridia. Therefore cooling between these temperature control points should be as rapid as possible.

1. During cooling, the product’s maximum internal temperature should not remain between 130°F (55oC) and 80°F (27oC) for more than 1.5 hours nor between 80°F (27oC) and 40°F (4oC) for more than 5 hours. This cooling rate can be applied universally to cooked products (e.g., partially cooked or fully cooked, intact or non-intact, meat or poultry) and is preferable to (2) below.

2. Over the past several years, FSIS has allowed products to be cooled according to the following procedures, which are based upon older, less precise data: chilling should begin within 90 minutes after the cooking cycle is completed. All products should be chilled from 120°F (48°C) to 55°F (12.7°C) in no more than 6 hours. Chilling should then continue until the product reaches 40°F (4.4°C); the product should not be shipped until it reaches 40°F (4.4°C). This second cooling guideline is taken from the former (“Requirements for the production of cooked beef, roast beef, and cooked corned beef”, 9 CFR 318.17(h)(10). It yields a significantly smaller margin of safety than the first cooling guideline above, especially if the product cooled is a non-intact product.

If an establishment uses this older cooling guideline, it should ensure that cooling is as rapid as possible, especially between 120°F (48°C) and 80°F (27oC), and monitor the cooling closely to prevent deviation. If product remains between 120°F (48°C) and 80°F (27oC) for more than one hour, compliance with the performance standard is less certain.

3. The following process may be used for the slow cooling of ready-to-eat meat and poultry cured with nitrite. Products cured with a minimum of 100 ppm ingoing sodium nitrite may be cooled so that the maximum internal temperature is reduced from 130 to 80° F in 5 hours and from 80 to 45° F in 10 hours (15 hours total cooling time).

This cooling process provides a narrow margin of safety. If a cooling deviation occurs, an establishment should assume that their process has exceeded the performance standard for controlling the growth of Clostridium perfringens and take corrective action. The presence of the nitrite, however, should ensure compliance with the performance standard for Clostridium botulinum.

From FSIS Directive 7117.0

1. Heat-resistant food-poisoning bacteria can grow from 38°F 3oC up to approximately 125°F (49oF); however their range of rapid growth is from approximately 80°F to 125° F. Thus, cooling product quickly through the rapid growth range is more important than cooling through the slow growth range.

2. The rate of heat transfer (cooling rate) from the product’s centre to its surface is directly proportional to the difference in temperature between those two points. Thus, as the product temperature approaches the coolant temperature, the cooling rate diminishes.

3. Traditional cured products, containing high amounts of salt and nitrite, together with low moisture content are more resistant to bacterial growth than similar newer products; some are even shelf-stable. Thus, rapid cooling of these traditional products is not always necessary. However, manufacturers are making fewer products of this type today. Instead, to meet present consumer tastes, most of their cured products contain less salt and more moisture. These changes minimize the inhibitory effect of added nitrite and increase the need to rapidly cool these products.” (Novak)

Water Cooling

The best way to cool sausages down is with water. Showering with cold water is a technique universally used. “Water removes heat much faster than air and hot products will drop their temperature fast. If a product was smoked such showering also cleans the surface of any remaining smoke particles and prevents shrivelling.” (Novak)

Let’s delve deeper into the science behind cooling. To do this we use Watts per meter-Kelvin (W/mK) or what is known as the ‘k Value’. It is the measure used to compare thermal conductivity. The k value, or Thermal Conductivity, is the rate of heat transfer in a homogeneous material. A k value of 1 means that 1m cube of a material will transfer heat at a rate of 1 watt for every degree of temperature difference between opposite faces. This will be given as 1 W/mK. The lower this value is, the less heat the material will transfer.

Chris and Steve James point out that “the thermal conductivity of processed meat products (including cured sausages and hams) range between 0.272 Wm-1K-1 at 22°C to 0.482 Wm-1K-1 at 80°C (Marcotte et al., 2008), whereas the thermal conductivity of water is 1 Wm-1K-1. Thus, the thermal conductivity of water is more than double that of most processed meats.”  Water sprayed onto the surface of a food product will act as a high conductivity path. 

Intermitted Spray Cooling

Chris and Steve James made their comments on a blog site related to intermitted spray cooling in response to someone claiming that water on the surface of a product acts as an insulator which is obviously incorrect not the case, as one can see when comparing the K value of the sausages and that of water. They stated that “the reason why intermittent spray cooling can have benefits over continuous spray cooling is that a break in spraying allows the water on the surface of the hot product to evaporate, thus enhancing the cooling effect.”

Panão (2008) investigated the physics involved in the heat transfer process using intermitted spray cooling. Their work has shown that small duty cycles promote heat removal by phase-change. They found that “as the duty cycle evolves toward the continuous spray condition, the cooling system’s thermal response improves, but phase-change is mitigated, affecting the system’s performance. Intermittent spray cooling is also compared with continuous spray cooling experiments and liquid savings has been estimated by 10–90% for the same energetic efficiencies reported in the literature.” They further recommend using shorter impingement distances and low injection pressures. (Panão, 2008)

Craig Habbick who has experience with these systems recommends the following procedure. Brine solution (water and salt) cooled to -5oC and sprayed intermittently altering 2 minutes to 1 minute off with circulation on during the spray off times. The entire cycle takes 15 minutes and reduces core temperature from 72oC to 2oC.

The concentration of salt was high. They used a Baume meter regulator to test the salt. Weight loss was so low that they had to remove water from the recipe due to seepage in the packs after packaging. Nett loss during cool down was around 2%. They used an Alkar brine chiller.

For details on the Alkar Brine Chiller, visit

The important graphs from the Alkar website are:


Novac remarks that there is no need to grab a water hose the moment the sausage was cooked in a smokehouse to 155° F (69°C) as this temperature lies outside the danger zone (40 – 140°F, 4 – 60°C). “U.S. regulations permit restaurants to hold cooked food at 145°F (63°C) or higher temperatures. However, once when the temperature of the product drops to 140°F (60°C), it should be cooled fast. The surface of a product such as a head cheese or smoked sausage both will benefit from a brief hot shower or immersing them in hot water. This will remove any possible grease from the outside and the product will look better. Then it will be showered with cold water. Some pork products may be cooked to > 137° F (58°C) just to eliminate the danger of contracting Trichinae. Such products should be cold showered immediately as they are already lying within the danger zone.” (3. Traditional cured products, containing high amounts of salt and nitrite, together with low moisture content are more resistant to bacterial growth than similar newer products; some are even shelf-stable. Thus, rapid cooling of these traditional products is not always necessary. However, manufacturers are making fewer products of this type today. Instead, to meet present consumer tastes, most of their cured products contain less salt and more moisture. These changes minimize the inhibitory effect of added nitrite and increase the need to rapidly cool these products.” (Novak)

Blast Chiller

We initially planned to have a blast chiller, but after the recommendation from Craig Habbick, the intermitted spray cooling system is so effective that there is no need for an air chiller (blast chiller).

Further Reading

The Alkar product Brochure


Jensen, W. K., Devine, C., Dikeman, M. (Editors), (2014), Encyclopedia of Meat Sciences, Second Edition. ISBN: 9780123847317. Elsevier.

Marcotte, M., Taherian, A. R. & Karimi, Y. (2008) Thermophysical properties of processed meat and poultry products.  Journal of Food Engineering. Vol. 88:3, pp315-322

Miguel R.O. Panão, António L.N. Moreira, Intermittent spray cooling: A new technology for controlling surface temperature, International Journal of Heat and Fluid Flow, Volume 30, Issue 1, 2009, Pages 117-130, ISSN 0142-727X,

Novak, J. Home Production of Quality Meats and Sausages

Photo Reference|

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Electrochemical Activation of Water and its use in the Meat Industry


Very early in my life, I was introduced to Electrochemically Activated Water through SAFIC (South African Fine Industrial Chemicals). Cyril Leibov and I developed a range of consumer chemicals with SAFIC which we took to the retail trade. The project was not successful but my introduction to ECA technology made a lasting impression on me. I am in Nigeria working on a meat project and in discussions about water, the topic of ECA came up. Still in South Africa, I came across this article, written in the Russian language. Using Google Translate, I did my best to translate it and paste it together again.

The technology is decidedly East European/ Russian and I am aware of very few researchers in the West who study its properties despite the fact that I know of a number of companies around the world offering ECA water as cleaning solutions.

The process is very simply described by the following diagram from Gluhchev, Georgi & Ignatov, Ignat & Karadzhov, Stoil & Miloshev, Georgi & Ivanov, Nikolay & Mosin, O.. (2015). Electrochemically Activated Water: Biophysical and Biological Effects of Anolyte and Catholyte Types of Water. European Journal of Molecular Biotechnology. 7. 12-26. 10.13187/ejmb.2015.7.12.

Below I give the fully translated article. I changed the language to convey what I thought was intended by the authors and since I do not speak the Russian language, if anyone come across mistakes that I made in my translation or interpretation and thus, inadvertently ascribed erroneous information to the authors, I offer my sincere apology and ask that you mail me with the corrections at or WhatsApp me on +27 71 5453029.

Article by:

Yakovenko NV, Komov IV Regional socio-economic-geographical systems: approaches to the definition // Network journal “Scientific result”. Series “Technologies of business and service”. – V.2, No. 1 (7), 2016.

INNOVATION IN FOOD PRODUCTION AND TRADE UDC 637.521:664.58664 DOI: 10.18413/2408-9346-2016-2-1-24-31

(1) Bal-Prilipko L.V., (2) Leonova B.I., (3) Naumenko L.V.

1) Dean of the Faculty of Food Technologies and Quality Management of Agricultural Products, Doctor of Technical Sciences, Professor. National University of Bioresources and Nature Management of Ukraine st. Colonel Potekhin, 16, Kiev, 03041, Ukraine. E-mail:
2) Candidate of Technical Sciences, Assistant of the Department of Technology of Meat, Fish and Seafood National University of Bioresources and Nature Management of Ukraine st. Colonel Potekhin, 16, Kiev, 03041, Ukraine. E-mail:
3) Master, National University of Bioresources and Nature Management of Ukraine st. Colonel Potekhin, 16, Kiev, 03041, Ukraine. E-mail:



The article presents the results of an analytical screening of the literature regarding the use of electrochemically activated water as the main component of brines in the production of meat products. Comparative analysis was carried out on the domestic and European requirements for the quality and safety of drinking water and the influence of water hardness, pH value and the redox potential of water on meat systems. Based on complex theoretical data, it is shown that the use of catholyte in the composition of brines eliminates the addition of chemical additives and components, improves the rheological properties of meat, makes the finished product environmentally safe with pronounced antioxidant properties. The electrochemical activation of water creates favourable conditions for its use in the meat industry.

Keywords: electrochemical activation, water hardness, pH value, ORP environment, antioxidants, metastable state, catholyte, anolyte, relaxation.


The article presents the results of an analytical screening of the literature regarding the use of electrochemically activated water as the main component of brines in the production of meat products. A comparison was made between domestic and European requirements for quality and safety of drinking water; it may have an influence on water-quality indicators such as water hardness, pH and redox potential in the meat system. Based on the comprehensive theoretical data it validates the use of the catholyte together with brines which has the potential to remove the need for certain chemical additives, improve the rheological properties of the meat, and makes the finished product environmentally safe with strong antioxidant properties. Electrochemical activation of water creates favourable conditions for its use in the meat industry.

Keywords: electrochemical activation, water hardness, active acidic pH, the redox potential of the environment, antioxidants, the metastable state, catholyte, anolyte, relaxation.


There is no question that water is an essential component of all food products. It influences quality, especially the consistency of water, moisture evaporation, hydrolytic and microbiological processes [2]. Due to the physical interaction of the water and the dissociation of hydrogen and hydroxyl ions of proteins, polysaccharides, lipids, and salts have a significant effect on the structure of the meat products [3]. The molecular weight of water is approximately equal to 18.02 [4] and it can exist in three states: liquid, steam, and ice. The main physical and chemical properties of water at 20 °C [5, 6, 7] are given in Table 1. (see table in the original text given below)

Water has the most mysterious and bizarre properties in nature. It can be said that water obeys her own laws of physics. When cooled below +4o water expands, instead of contracting, as is typical of other substances in the transition from a liquid state to solid.

Water has a high surface tension, a dielectric constant, heat capacity and thermal conductivity. Modern science explains its uniqueness because water molecules have the property of uniting into complex polyassociative structures – clusters, which form hierarchical spatial liquid crystal structures which receive and store information.

To compare the requirements for indicators of quality and safety of drinking water of Ukrainian and European regulatory documents were analyzed and the results are presented in Table 2. (See table in the original text given below)

A feature of drinking quality standards of water, established by EU Directive No. 80/778, is the regulation of the values of the “maximum allowable concentration”. This group sets standards that should provide an increase in the level of drinking water safety and improve organoleptic characteristics, and which in the development of new improved water treatment systems and technical (analytical) quality controls should be seen as promising indicators of drinking water quality.

The analysis carried out showed a large discrepancy between Ukrainian and European standards, especially regarding water hardness. Having said this, it should be noted that hard water is one of the most important problems for the domestic meat industry. It has been shown that regularly consuming hard water, leads to a decrease in the functioning of the stomach, the accumulation of salts in the body, and, to joint disease (arthritis, polyarthritis) and the formation of stones in kidneys and bile ducts. On the other hand, very soft water can also negatively affect a person’s body by reducing bones calcium and removing minerals and bacteria from the digestive tract.

Thus, the optimal harness level of water has been established for drinking water as between 2 – 5 mg/L. Furthermore, for the business and for equipment, the use of hard water is associated with entails many negative consequences such as plaque formation on plumbing fixtures, water heater systems, fittings, and equipment. Hard water leads to an increase in the use of soap and detergents due to the presence of calcium and magnesium salts of fatty acids. Unfortunately, in the meat processing industry technology is lacking to soften hard water.

It was found that the pH of water impacts the water-binding capacity (WBC) of meat, the oxidation rate of myoglobin leading to altering the colour of meat products and other physicochemical and biochemical processes. The bright colour of salt-cured meat is dependent on the pH value, which in turn depends on the pH of the water and additives used in the preparation of the brine. To improve the colour of meat products it is necessary to create optimal oxidizing recovery conditions. To achieve desired results, the meat industry generally uses organic acids such as ascorbic, wine, dairy, lemon [8]. The pH value of the meat system has a considerable influence on the rate of the nitrosation process and the level of residual nitrite in the product [9]. When compiling protein-carbohydrate compositions to produce meat products, the pH of the water affects the nature of the protein-water interaction. It is known that alkalization of the environment increases the degree of hydration of proteins and increase water-binding and the emulsifying ability of the protein [10]. In the meat industry, phosphates and their mixes are used for this purpose [11, 12, 13].

The German scientist, L. Leistner, the father of the theory of hurdle technology, used specific contributors to food quality, safety and to extend the shelf life of food, classifying ORP and the medium pH as two of his six major hurdles [14]. According to theory, for any long shelf-life food product which remains safe to consume, multiple hurdles (factors) must exist to control the number of microorganisms in this product. So, for the product to remain safe, microorganisms present at the beginning of production, should not be able to overcome these barriers.

Usually, to change the pH and ORP of water various chemicals and additives are employed. There is, however, a growing interest in electrochemical activation, since its use allows the regulation of both these factors across a wide spectrum without introducing more and often unwanted chemical elements to the system to decrease the hardness of the water [17, 18, 19, 20, 21, 22, 23, 24].

The oxidation-reduction potential is a measure of the ability of chemical/biochemical systems to oxidize (lose electrons) or reduce (gain electrons) or the electron-acceptor or electron-donor properties of biological media regarding their own endogenous components and substances of exogenous origin. In other words, it characterizes the measure of electron activity of receiving electrons and is reduced or donating of electrons and is oxidised. In humans, ORP is in the range between -200 to +200 mV [25]. Media with a positive ORP have electron-acceptor properties, and when ingested, it increases the oxidative load and leads to the disruption of peroxide homeostasis. Antioxidant substances have the ability to reduce ORP. In turn, such an ORP shift provides thermodynamic conditions for the transition of oxidized compounds to reducing forms [26].

In terms of the therapeutic effect of antioxidants, it blocks the formation of compounds such as oxidized fatty acids, peroxides, aldehydes, and ketones in the tissues of organisms [27, 28]. As a result, there is an enrichment of the total pool of recovered compounds in the body. As is well known, the natural antioxidant system of humans is a well-balanced antiradical chain of antioxidant agents that transfer protons and electrons from metabolites – participants in enzymatic oxidation of free radical compounds. ORP performs exactly this function of the regulation of the transport of protons and electrons.

Antioxidant properties are inherent in substances such as histamine, cysteine, arginine, glutathione, thiourea, glutamic acid, vitamins E, B, C and others. Glutathione is made up of residues of glycine, cysteine, and glutamine acids [29], present in plant tissues, microorganisms, and animals in both oxidized and restored forms. Arginine can actively absorb superoxide radicals [30] and manifests itself both at the beginning and in the development of the free radical chain oxidation. Vitamin C is characterized as having the ability to reverse oxidative damage through restorative transformations.

Regarding meat as a raw material to produce meat products, the effect of antioxidants is in the prevention of lipid oxidation which happens when divalent metal ions bind to meat and blood pigments. For this, the most widely used vitamins of group E, lemon, ascorbic, apple and amber acids [1], as well as propyl gallate, pyro- and tripolyphosphates, rosemary, soybean oil, cardamom, mustard, coriander, red pepper, and extracts obtained on their basis [31, 32]. Electrochemically activated water has a beneficial impact on the whole organism. Drinking water with a negative ORP is easily absorbed by the body, giving it its free charges, and thus stimulating physiological regenerative processes. As a result of electrochemical activation, water enters a metastable state, which is characterized by abnormal values of physical and chemical characteristics, including ORP, electrical conductivity, acid-base balance. Catholyte is light, alkaline, sometimes with white precipitate, water with a pH close to 10-11, and an ORP of equal to -200 to -800 mV; anolyte is brown, sour, with a characteristic smell, pH 4-5, and an ORP range of between +500 to +1100 mV [16, 17].

Important characteristics of activated solutions are pH and ORP, an inherent change of these characteristics over time (relax) even when there is a lack of mass exchange with the environment. That is, the anomaly of the solution disappears, and the water returns to its classic thermodynamic equilibrium. So it is advisable to use it immediately after electrochemical processing.

ORP of the water is less stable, unlike pH, especially related to the catholyte, and directly depends on external conditions (light, temperature, vessel material, surface area contact with air, etc.) [24].

In several works, it is noted that the catholyte in normal conditions and in a state of relative rest does not relax during the first two hours [33, 34]. To extend the relaxation time, the catholyte needs to be stored and transported in tightly closed and containers should be filled to the top with it. Subject to the data rules, it will not change its characteristics for 2-3 days. The anolyte can be stored in an open or closed container (except for copper) for a long time (weeks, months). It is important to remember that acceleration of relaxation is facilitated by mixing with air, spray overflow, a small volume of liquid [35]. A key last role in this process is played by the mineralization of the original water. Freshwater anolyte loses its biocidal ability, unlike an anolyte of a concentrated solution. When mixing anolyte and catholyte in an equivalent ratio a non-activated solution is created, like the properties of hypochlorite [33].

Anolyte has enough strong oxidizing agents and free radicals, therefore, its solution becomes a strongly pronounced biocidal agent. Even if diluted in ordinary water with a concentration 1:40, it prevents the development of such microorganisms like Staphylococcus aureus, salmonella, E. coli; 1:8, mushrooms of the genus candida, etc. [29]. Catholyte as a reducing agent due to its high adsorption chemical ability also has strong detergent properties. It is interesting that a catholyte with weakly expressed electron donor properties (ORP more than -400 mV) is ineffective, and a catholyte with excess electron-donor properties (ORP is less than – 400 mV) has an antimetabolic ability. It is known from research data [24] that in the case of ionizing radiation, catholyte manifests itself as an effective radioprotector, while the anolyte accelerates the course of the radiation diseases and enhances the lethal effects of radiation. No carcinogens are found in activated solutions, and it is not carcinogenic, and it has no allergic or toxic effect on the human body intravenous, intramuscular, intra-abdominal, subcutaneous, and orally administered. As noted earlier, the abnormal properties of electrochemically activated water create favourable prerequisites for its use catholyte in the production of meat products.


Analyzing data from the literature on the use of activated water in the meat industry, we can draw the following conclusions and assumptions:

– the use of electrochemical process activation makes it possible to regulate the pH and ORP in the meat systems, eliminate various chemical additives and components. It has great application in raw meat with signs of either PSE or DFD. In addition, the pH and ORP values systems affect the formation of colour;

– alkaline pH value of the catholyte has positive effects when used in protein-carbohydrate formulations in the composition of brines for meat products, as it contributes to an increase in the degree of hydration of protein particles, increases emulsifying and water-retaining protein ability. As a result, it eliminates the need to use phosphates and their mixtures.

– because of the decrease of water hardness in electroactive water and its highly toxic elements and heavy metals, it is important from an environmental safety perspective of the finished product.

– the product obtained by using the catholyte with an abnormally low-value ORP (up to -800 mV), possesses antioxidant properties that prevent and reduce lipid oxidation of meat raw materials.

– due to increased wettability and the dissolving power of the catholyte, the preparation of emulsions and brines are faster and more effective.

– due to the increased penetrating ability of the catholyte the salting process is sped up and salt cost reduced, even increasing the quality of the process itself.

– due to catholyte activation, the action of tissue enzymes on the tissue, the muscle structure is improved and the rheological properties of meat. The product becomes more juicy, tender, and fragrant.

Original Article


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10) Barybina, L. I. Development of technology functional meat products with using dairy protein-carbohydrate concentrates: diss. PhD. [Text] / L. I. Barybina. Stavropol, 2001. 212 p.

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/ Yu. B. Zimin, B. P. Likachevsky, I. V. Kutsy // Meat industry. 2000. No. 2. S. 43-44.

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20) Bakhir, V. M. Electrochemical activation
[Text]. Part 1 / V. M. Bakhir. M. : VNIIIMT, 1992.
pp. 189-195.

21) Borisenko, AA Theoretical and practical aspects of polyfunctional use of electroactive fluids in technological processes of producing meat products: diss. d.t.s. [Text] / AA Borisenko. Stavropol: 2002. 472 p.

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24) Vasiliev, R.A. Possibilities of use activated water in sausage production: express inform. [Text] // Meat and refrigeration industry. M. : AgroNIITEI myasomolprom. Issue. 6. S. 7-10.

25) V. I. Prilutsky, Electrochemical activated water: anomalous properties, mechanism biological action [Text] / V. I. Prilutsky, V. M. Bakhir. M.: VNIIMT, 1997. 244 p.

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28) Klimanov, A. K. Complex solutions production and packaging of semi-finished products [Text] / A. K. Klimanov, T. B. Shugurova // Meat industry, No. 9. S. 39-42.

29) Ushkalova, V. N. Lipid stability food products [Text] / V. N. Ushkalova. M.: Agropromizdat, 1988. 152 p.

30) Khalmetov, R. Kh. Antimicrobial properties neutral anolyte obtained at the plant STEL [Text] / R.Kh. Khalmetov, M.T. Takhirov, A.Kh. Kasymov et al. // Electrochemical activation in medicine, agriculture, industry. No. 14.

31) Bordun, I.M. relaxation processes in electrochemical activation of water [Text] / I. M. Bordun, V. V. Ptashnik // Shidno-European Journal of Advanced Technologies. 2012. No. 1/6 (55). pp. 27-31.

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33) Prilutsky, V. I. Electrochemical STEL units: performance characteristics, application in medicine [Text] / V. I. Prilutsky, Yu. G. Zadorozhny // Electrochemical activation in medicine, agriculture, industry. 1999. No. 14. http://misrt. (access date: February 15, 2016).

34) Application of electroactive water in poultry farming: guidelines [Text] / [V. I. Filonenko, V. G. Shol, V. I. Fisinin and others]. Sergiev Posad, 1995. 46 p.

35) Shol, V. G. Relaxation of electroactive flat water. [Text] / V. G. Shol, V. I. Filonenko, V. A. Ofitserov, O. V. Bogatov // Abstracts. report All-Russian Conf. “Methods and means sterilization and disinfection in medicine. M.: MISRT, S. 63.

36) Mosin, O. V. Pi-water (micro-water) [Electronic resource] / access mode (accessed: 02/10/2016).


1) Pasichnyy, VM Perspective directions of production of meat and meat semis plant [Text] / V. M. Pasichnyy // Meat Case. 2009. No. 8. Prop. 15-19.

2) Borisenko, L.A. Modern methods of quality properties of reagentless control of meat products [Text] / [LA Borisenko, CD Shestakov, AA Borisenko and others // Meat series. 2007. No. 4. Prop. 22-23.

3) Bal-Prilipko, L. V, Leonova B.I. Mathematical modeling of stabilizing processes for activated water environs [Electronic resource] / access mode (date of
access: 10.02.2016).4)

4) Poznyakovsky, VM The use of vitamins in the production of meat products: Survey information [Text] /
VM Poznyakovsky, AN Bohatirev, VB Spirichev. M. : AgronIITEIMMP, 1986. 24 p.

5) Bolshakov, AS Technological properties of activated water [Text] / AS Bolshakov, LA Saricheva, AA Borisenko // Proceedings of the universities. food technology. 1992. No. 2. Prop. 56-58.

6) Nechaev, AP Food Chemistry [Text] / AP Nechaev, SE Traubenberg, AA Kochetkova / Ed. A.P. neChaev. SPb. : GIORD, 2003. 640 p.

7) Rogov, IA Disperse systems of meat and dairy products [Text] / IA Rogov, AV Gorbatov, VY Svintsov. M. : Agropromizdat, 1990. 320 p.

8) Zayas, YF Quality of meat and meat products [Text] / Zayas UFM: Easy and food industries, 1981. $480

9) Chirkina, TF Role of food additives in increasing the quality of canned meat: Survey information [Text] / TF Chirkina, VI Khlebnikov. M. : TSnIITEI Myasomolprom, 1986. 29 p.

10) Barybina, L.I. Development of technology for meat products of a functional purpose with milk proteincarbohydrate concentrates: diss. cts[Text] / L.I. Barybina. Stavropol, 2001. 212 p.

11) Zimin, YB Applying of German food phosphates in the production of meat products [Text] / YB Zimin, BP Likachevsky, IV Kutsyy // Meat industry. 2000. No. 2. Prop. 43-44.

12) Sokolov, A. A. Physical-chemical and biochemical bases of technology of meat [Text] / Sokolov AA M . : Food Industry, 1965. 490 p.

13) Technology of meat and meat products [Text] / [LT Alekhina, AS Bolshakov, VH Boreskov and others]; ed. I. A. Rogov. M. : Agropromizdat, 1988. 576 p.

14) Leistner, L. Hurdle effect and energy saving. In Food Quality and nutrition [Text] / L. Leistner. London : Applied Science Publishers, 2002. 553 p.

15) Bochinsky, AA Basic indicators of influencing on storage periods cooked meats [Text] / AA Bochinsky, ID Perepletchikov // Meat Industry. 1998. No. 6.
Pp. 21-22.

16) Vagin, VV Phosphates “Albright & Wilson” as a means to reduce the cost of meat products [Text] / VV Vagin, DP Martashov // Meat Industry. 1999. No. 2. Pp. 37-38.

17) Gorbatov, VM Activated aqueous solutions and possibilities of their application in the meat industry: Survey information [Text] / VM Gorbatov, n. A. Pirogovskiy, AB Khakimdzhanov, VL Knyazeva. M. : TSnIITEI Myasomolprom, 1986. 47 p.

18) Alekhin, SA new technologies based on electrochemical activation [Electronic resource] /

19) SA Alekhin. M. : MIS-RT. 1998. No. 3. http: // www misrt. Ru (date of access: 15.02.2016).

20) Bahir, VM Electrochemical activation of aqueous solutions and its technological applications in the food industry: Survey information [Text] / VM Bahir, n. G. Tsikoridze, LE Spector. Tbilisi: GruznIInTI, 1988.

21) Bahir, VM Electrochemical activation. Part 1 / VM Bahir. M. : VNIIMT, 1992. Prop. 189-195.

22) Borisenko A.A. Theoretical and practical aspects of multifunctional use of electroactivated liquids in technological processes of production of meat products: diss. Doctor of Science [Text] / A.A. Borisenko.
Stavropol: 2002. 472 p.

23) Borisenko, L.A. Scientific and technical bases of intensive technologies of salted meat raw materials with using ink jet of injection method for multicomponent and activated liquid systems: Author. diss. Doctor of Science [Text] / LA Borisenko. M. : 1999. 49 p.

24) Vasiliev, RA Possibilities of use of activated water in sausage production: Express-Inform [Text] // meat and refrigeration industry. M. : AgroNIITEI Myasomolprom. 1988. Issue no 6. Prop. 7-10.

25) Prilutsky, VI Electrochemically activated water: anomalous properties, mechanism of biological action [Text] / VI Prilutsky, VM Bahir. Moscow: VNIIMT, 244 p.

26) Prida, AI natural antioxidants of polyphenol nature. (Anti-radical properties and prospects of use) [Text] / AI Prida, RI Ivanova // Food Ingredients. Raw materials and additives, 2004. No. 2. Pr. 76-78.

27) A new look at organic acids [Text] // Meat Technology, 2007. No. 10. P. 26-27.

28) Klimanov, AK Complete solutions production and packaging semi-finished [Text] / AK Klimanov, TB Shugurova // Meat Industry, 2006. No. 9. Prop. 39-42.

29) Ushkalova, V. n. The stability of lipids food products [Text] / V. n. Ushkalova. M. : Agropromizdat, 152 p.

30) Khalmetov, RH Antimicrobial properties of neutral anolyte produced in STEL [Text] / RH Khalmetov, MT Tahirov, AH Kasymov and others // Electrochemical activation in medicine, agriculture and industry. 1999. No. 14.

31) Bordun, IM Effect of storage conditions on the relaxation processes in electrochemically activated water [Text] / IM Bordun, VV Ptashnyk // Eastern European Journal of advanced technologies. 2012. No. 1/6 (55). Pp. 27-31.

32) Bahir, VM Factors of reactivity of electrochemically activated solutions [Text] / VM Bahir, E. A. Repetin // Proc. rep. All-Russian conf. «Methods and means of sterilization and disinfection in medicine” M . : MIS-RT, 1992. No. 12. Prop. 8-13.

33) Prilutsky, VI Electrochemical STEL: operating characteristics, application in medicine [Text] / VI Prilutsky, YG Zadorozhnyy // Electrochemical activation in medicine, agriculture and industry. 1999. No. 14. (date of access: 02/15/2016).

34) Applying the electro-activated water in the poultry industry: methodical recommendations [Text] /
[VI Filonenko, VG Shol, VI Fisinin and others]. Sergiev Posad, 1995. 46 p.

35) Shol, VG Relaxation electroactivated water [Text] / VG Shol , VI Filonenko, VA Ofitserov,
OV Bogatov // Proc. rep. All-Russian conf. “Methods and means of sterilization and disinfection in medicine”. M. : MIS-RT, 1992. P. 63.

36) Mosin, OV Pi-water (micro water) [Electron resource] / access mode (date of access: 02/10/2016).

The Processing of Animal Bones

By Eben van Tonder
28 January 2022


For several years now I have been looking into the use of the 5th quarter from animal slaughtering to find ways to use this more effectively in human nutrition. Despite legislative challenges which classify, for example, animal bones as inedible, thorough investigations have been carried out over the years which clearly show such legislation to be outdated and ill-informed. In other instances, it is due to mostly Western prejudice against the consumption of certain parts of the animal which made its way into legislation.

Some animal parts classified as in-edible in Western countries are customarily used in several non-Western countries as human food such as beef hides which is consumed in Nigeria as Ponmo (Kpomo). An attempt is being made in some Western countries to find a way past the outdated and ill-informed legislation by having such food classified as traditional dishes.

Homemade Roasted Beef Bone Marrow with Thyme and Lemon

An even more surprising situation exists in a country like South Africa where it seems as if the authorities frown upon attempts to even investigate the use of these by-products in food processing. When they make their case, they do not refer to science, for example, to try and show that certain animal parts are harmful when consumed but to legislation in Western countries as if this is anything to go by. The unambiguous evidence of mounting research data is that consuming a great percentage of these so-called in-edible parts of a carcass is not dangerous to humans. On the contrary! It turns out to be highly nutritious and their inclusion in, for example, sausage formulations will add to the nutritional characteristics of the food and lower prices.

Over the last few years equipment has become available to process certain animal by-products in such a way that nutrition is enhanced by increased bioavailability, mostly through a greater degree of comminution. Disruptor technology has for example been pioneered in South Africa which reduce the particle size of these by-products dramatically. Ultrafine grinding of bones has become possible through a range of equipment and processes. The high-volume processing of such material will undoubtedly have to be done through equipment like the Dynamic Cellular Disruption (DCD) process, pioneered by Green Cell Technologies (GCT), but smaller machines for small processing are available.

This means that from the perspective of nutrition (backed up by thorough scientific research) and equipment, there is no longer any reason to maintain the archaic Western-focused aversion to the processing of the entire carcass and including most of it in food produced for human consumption should be legislated. In countries where bones and animal hides have not been classified as inedible, the status quo should remain unchanged for the benefit of the respective populations, culturally, nutritionally, and as far as affordability is concerned. From a philosophical perspective, it is my opinion that not utilising the full carcass for human nutrition shows great disrespect to the animal by somehow implying that certain parts are only good to feed other animals or fertiliser.

Animal Bones are Nutritious.

Horizontal composition of a roasting tray full of roasted beef marrow bones grilled to golden perfection

The first point that must be made about bones is that it is already part of human food in the form of broth and soups. If we just pause there and realise that in South Africa it’s classified as not fit for human consumption we can ask, so are we or are we not allowed to sell “meaty bones” (as is being done), as soup bones? So, the legislature allows it because this is an extremely popular South African product, despite being described, technically, as “not fit for human consumption.” So much so that the bones are no problem in South Africa and sell at such good prices that producers give bones not a second thought. The market exists for it by simply cutting it up with a bandsaw into smaller chunks.

Chicken bone is another example that is much softer than other animal bones and comes to us through MDM. In some countries in Africa, MDM is banned for no good technical reason and as far as Europe is concerned, it is a completely different reason which is beyond the scope of our current discussion.

Back to the South African example. We are allowed to sell all the bones in the entire country to be used in soups and we are allowed to use MDM which are packed with chicken bones, still using bone meal as is produced for animal feed around the world in food for human consumption will be a problem for the South African legislator.

These inconsistencies in handling the matter aside, the reality is that bones are packed with nutritional elements. The fat and protein content is, however, not parallel to that found in the rest of the body as some authors suggest. Paloheimo (1965) reported that the bone-free body of one of three Paloheimoof dairy cows analysed contained 25.2 % fat while the corresponding figure of the skeleton was 19.9. The second cow gave figures 15.5 and 22.0 respectively, and the third 14.7 and 19.0. They continued their study and analysed specific bones as opposed to the whole carcass bones as in the three dairy cows. The average percentage from the femurs of 20 cows and 4 young animals, where fat, protein and ash were directly determined and the water content was calculated as the difference, are as follows (ranges of variation given in brackets).

Fat 33.6 (26.9 – 38.9)
Protein 17.2 (15.0 – 21.6)
Ash 34.8 (33.0 – 33.9)
Water 14.4 (11.3 – 16.0)

Bones serve amongst others, as a reservoir of calcium and phosphate ions for the entire body. It is “composed of various types of cells and collagenous extracellular organic matrix, which is predominantly type I collagen (85–95%) called osteoid that becomes mineralised by the deposition of calcium hydroxyapatite. The non-collagenous constituents are composed of proteins and proteoglycans, which are specific to bone and the dental hard connective tissues.” (Mohamed, 2008)

Yessimbekov (2021) investigated the use of meat-bone paste to develop calcium-enriched liver pâté. They found that “the compositional analysis of pâté manufactured with meat-bone paste showed that the reformulation did not influence the content of moisture (~56%), fat (~28%), or protein (~11%) while producing a significant increase of ash and a decrease of carbohydrates in comparison with control pâtés. The higher amounts of minerals of bone-meat paste, including calcium (3080 mg/100 g), magnesium (2120 mg/100 g), phosphorous (2564 mg/100 g), and iron (7.30 mg/100 g), explained the higher amount of both ash and these minerals in the reformulated samples compared to the control samples.”

The total caloric value (~300 kcal/100 g) was unaffected by the addition of bone-meat paste. “The content of both essential and non-essential amino acids decreased with the inclusion of meat-bone paste, although this decrease was lower in essential (6280 mg/100 g in control vs. 5756 mg/100 g in samples with 25% of meat-bone paste) than in non-essential amino acids (6080 mg/100 g in control vs. 3590 mg/100 g in samples with 25% of meat-bone paste). This fact is due to several essential amino acids not showing differences between control and reformulated samples, while in non-essential amino acids, these differences were greater.” (Yessimbekov, 2021)

“The results of this study showed that meat-bone paste addition is a good strategy to produce liver pâté enriched in minerals and with minimum influence on the content of the other important nutrients. Therefore, these results can be used for the design of new liver pâté with an increased nutritional significance by using meat industry by-products. According to the balance of minerals, the use of 15% of meat-bone paste to reformulate liver pâté is the best strategy used in the present research.” They caution that “additional studies on the stability (during storage), shelf-life, and sensory acceptability of these reformulated pâtés should be carried out.” (Yessimbekov, 2021)

Kakimov (2017) states that “bones are rich in mineral elements (in particular, calcium, phosphorus, magnesium and iron), protein (collagen) and fatty substances. Bone consists of 13.8 – 44.4% water, 32 – 32.8% protein (collagen), 28.0 – 53.0% mineral elements and 1.3 – 26.9% fat. The most characteristic components of bone are mineral elements, represented by calcium carbonate and phosphoric acid, followed by various oxides (%) (CaO 52, MgO 1.2, P2O5 40.3, Na2O 1.1, K2O 0.2, Cl 0.1, F 0.1 and CO2 5.0). Cattle bones, which contain between 9 and 14 mg kg–1 calcium are a major source for calcium and phosphorous salts.” They quote Drake et al., that “bone is a useful calcium source for nutrition because bone particles are readily dissolved by gastric juices. Moreover, the use of mineral salts in the production of meat-based products enables enrichment of food with mineral supplements, particularly calcium, phosphorous, magnesium and other elements that can be helpful in preventing diseases associated with mineral deficiencies, such as osteoporosis”. (Kakimov, 2017)

They state that “meat-bone meal can provide a rich source of whole protein and is an especially rich source of the essential amino acid lysine, as well as mineral supplements. For human consumption, bone is typically used to prepare protein hydrolysates and mineral supplements, bone broth and bone fat.” (Kakimov, 2017)

Kakamov (2017) describes a superfine bone grinding processes beginning with “crushing the bone to 1-3 mm particles followed by ultra fine grinding to yield 50-100 mm particles can be used to make paste-like products that have a soft texture and are fully digestible by humans.” He notes that such pastes can be used for the production of food supplements and different meat products such as sausages, pates and semi-finished meat products. Moreover, since the meat-bone grinding process does not involve thermal treatments, the vitamin, mineral and protein content is preserved

Kakimov (2017) evaluated the meat-bone paste (MBP) as an ingredient for meat batter and its effect on physicochemical properties and amino acid composition. They developed five formulations, a control and “four meat batters with different amounts of MBP, 10% (MBP-10), 20% (MBP-20), 30% (MBP-30) and 40% (MBP-40), respectively. The active acidity (pH) of the formulations was determined by potentiometry. Samples were analyzed for water binding capacity (WBC) by exudation of moisture onto filter paper following the application of pressure. The amino acid composition was determined by liquid chromatography.” (Kakimov, 2017)

Bone Paste Preparation

A pewter serving dish arranged with slow-cooked beef bones split to reveal the delicious marrow seasoned with onion, chiles, cilantro, served with hot fresh corn tortillas at a restaurant in Juarez

Kakimov (2017) summarises current processing methods as usually involving “grinding and hydrolysis of the bones, followed by treatment with various chemical reagents.” He references Berdutina and Antipova et al. who “describes the preparation of protein hydrolysates from bone that included fermentation and acid hydrolysis.” “For a study on the production of protein supplements,” Kakimov (2017) references Kutcsakov et al. who describes “hydrolysis of meat-bone raw material by hydrochloric acid followed by sodium hydroxide neutralization, defatting and drying.”

Yessimbekov (2021) mentions that a patent has recently been granted on one such process. “A patent was granted by the Republic of Kazakhstan #2202 on 15 June 2017 for the method developed by Kakimov et al.. Bone grinding processing by this procedure allows obtaining a meat-bone paste which is free of hard bone particles; thus, it results in a product that is smooth and soft to the tongue of the consumer.” (Yessimbekov, 2021)

“Bones with meat tissue were washed with cold water and then crushed into 50 –70mm long fragments. Cutting bones into small pieces was done manually with an axe. The bone fragments were stored at -18oC to – 20oC before loading into the hopper of a crushing machine equipped with an 8mm diameter meat grinder plate. The bone was ground and crushed again using a 3mm meat grinder plate; water was then added to a 1:1 ratio (w/w). The mixture was frozen at -3oC to -5oC for 1 h and then ground using a micro-milling machine having rotational knives spaced at 0.50mm. The resulting meat-bone paste (MBP)
was used to prepare pâté meat batters.” (Yessimbekov, 2021)

Kakimov (2017), to study the meat-bone paste as an ingredient for meat batter and the effect on physicochemical properties and amino acid composition used bones with attached meat tissue and “washed [it] with cold water and then crushed [it] into 50-70 mm long fragments. The bone fragments were stored at 18-20°C before loading into the hopper of a crushing machine V2-FDB (Russia) equipped with an 8 mm diameter meat grinder plate. The bone was ground and crushed again using a 3 mm meat grinder plate, water was then added to a 1:1 ratio (w/w). The mixture was frozen at -3 – 5°C for 1 h and then ground using a Supermasscolloider MKZA-10-15 (Masuko Sangyo Co., Ltd, Kawaguchi, Japan) micromilling machine having rotational knives spaced at 0.5 mm. The resulting meat-bone paste (MBP) was used to prepare meat batters.”

The meat batter they prepared was done as follows. “Five meat batter formulations were prepared using varying amounts of MBP and prime and grade one beef from which all visible connective tissue was removed. The mixtures were then ground by passage through a meat grinder fitted first with an 8 mm plate and then a 5 mm plate. The basic composition of the meat batter was 50% prime beef, 35% grade one beef (together, a total of 85% beef), 10% ground boiled beans and 5% egg mélange. Then, MBP was substituted for the prime and grade one beef mixture at four amounts 10, 20, 30 and 40%, respectively. Meat batters were prepared in a mixer-cutter to which the minced meat, MBP, boiled beans, 2.5% sodium nitrite, egg mélange and water were added individually. All the ingredients were mixed and ground together for 5-10 min at 2-4°C. Salt was added to extract myofibrillar proteins, whereas egg mélange was included as an emulsifier to bind the meat batter components, as well as a source of unsaturated fatty acids and lecithin. For seasoning, peeled and minced garlic, granulated sugar, black or white pepper and coriander were added. Sodium nitrite was included as a preservative. After mixing, the meat batters were packed in polyethylene bags and stored at (-8°C).” (Kakimov, 2017)

The following table shows the composition of the different meat mixes.

Graph from Kakimov (2017)


Bone-Paste Particle Size

The waiter is holding a plate Beef bone marrow with chimichurri sauce and toasted bun. Served on a chopping wooden Board. Menu BBQ restaurant.

Yessimbekov (2021) reports that “as can be seen in the image of bone particles, magnified 50 times where the bone particle sizes were measured, particle sizes exceeding 0.40 mm (400 microns) were not detected.

Bone particle sizes of meat-bone paste by Yessimbekov (2021).

“On the basis of the sieve analysis of the meat-bone paste after grinding on a colloid machine with a gap between the grinding wheels of 0.10 mm, it was found that the mass fraction of bone particles ranging in size from 0.10 mm to 0.25 mm is more than 95%. Bone particles that were beyond 0.25 mm were less than 5% and, as mentioned, particles of 0.40 mm (or higher) were not detected. Similar findings were obtained in a previous study, in which the meat-bone particle size after grinding on the colloid mincing machine was from 0.20 to 1.5 mm, while after grinding on the superfine machine, the particle size was reduced to less than 0.10 mm. A more recent study concluded that after grinding in the masscolloider with a gap of 0.25 mm, the bone particle size ranged between 0.14 mm and 0.37 mm, while after using a masscolloider with a gap of 0.10 mm, the bone size decreased and ranged between 0.045 mm and 0.19 mm. These results agree with our findings, and they demonstrate that the process and conditions for obtaining the meat-bone paste are good and that this allows obtaining a meat-bone paste with a smooth texture, which is not perceptible by consumers, and which is digestible by humans. Therefore, the meat-bone paste obtained in this research can be used for the production or reformulation of meat products: in our case, liver pâté.” (Yessimbekov, 2021)

Results from Kakimov Meat-Bone Batters

A high-angle close up photograph of a gourmet beef bone marrow dish served with toast and a herb salad

“Proximate composition of the meat-bone paste (MBP) was determined. Relative to the base formulation (control), MBP had a higher ash level (15.99±0.18%) but a lower fat (4.35±0.06%) and protein (14.70±0.17%) content and a moisture level of 64.97±0.79%. The effect of increasing amounts of MBP on the proximate composition of meat batters (table above) was analyzed. At 40% MBP (MBP-40), the ash content significantly increased relative to the control (5.24 vs. 0.81%), whereas the protein and fat content steadily decreased with increasing amounts of MBP. In particular, the fat content of the control sample fat content was 16.50% but the MBP-40 batter had only 10.71% fat. Meanwhile, MBP-40 had a lower protein content than the control, which was slightly but not significantly, lower than that of MBP-10 (16.26, 17.49 and 17.67%, respectively). The moisture content of the samples ranged from 65.20 – 67.79% and there were no significant differences among the formulations. The energy value of meat batters steadily decreased with the addition of MBP, with MBP-40 having the fewest calories per 100 g.” (Kakimov, 2017)

“The ash content of the MBP-30 and MBP-40 formulations was markedly higher (4.18 and 5.24%, respectively) than the recommended amount for meat batters (approximately 3.5%). Similar trends in moisture, fat and protein (64.17, 17.83, 16.68%, respectively) content were observed in a study by Kahramanov for meat batters made from grade two beef, fermented meat trimmings and blood. Except for the ash content, the proximate composition of these meat batters was also similar to that observed by Kakimov, who developed a protein supplement (protein 15.39%, fat 12.94% and ash 1.41%) for meat batters consisting of bone fat, blood, egg mélange and ultrafine ground bone. In another study, Pershina showed that bone powder added to a sausage formulation that included beef, pork, milk and eggs resulted in sausages that had a lower protein content (12.0-14.0%) and higher fat content (18-22%), which both differed from those seen for this study. Krishnan and Sharma used offal meat (rumen and heart meat) to process cooked sausages that had a protein content similar to the MBP-40 formulation (16.39% vs. 16.26%), whereas meat patties composed of ground beef and 10% spleen tissue in a study by Bittel and Graham had significantly higher protein content (26%) than it was seen with our formulations. Overall, however, the proximate composition of the meat batter was consistent with that observed for previous studies.” (Kakimov, 2017)

WBC and pH Determination: 

Close up of rustic English bone marrow, pickled onion and toast on a basalt plate

“The pH is an important parameter that can significantly impact sensory, microbiological, physicochemical and rheological characteristics of meat and meat products. The addition of MBP raised the pH of the meat batter, with more neutral pH values seen for MBP-40 vs. the control (6.20 vs. 7.26). This effect is likely because the MBP itself has a high pH (7.28). The WBC also changed with the addition of increasing amounts of MBP as evidenced by the sharp and significant increase in WBC of more than 15% between MBP-10 and MBP-20. The increase can be attributed to the high water binding capacity of MBP.” (Kakimov, 2017)

WBC and pHin meat batter with different proportions of meat-bone paste. (Kakimov, 2017)

Effect of MBP on pH and water binding capacity (WBC) of meat batters. *Indicates that the values are statistically different from control (*p<0.05, **p<0.02). Results are Mean±SD

Amino Acid Determination

Roasted beef bone marrow with butter and French toast

“The MBP also changed the total amino acid content of the meat batter formulation. Amino acid composition of MBP showed the large amount of glycine (2556.28 mg/100 g), proline (1649.32 mg/100 g) and oxyproline (1360.75 mg/100 g).” (Kakimov, 2017)

Amino acid composition of meat batters, mg/100 g of product

“These amino acids constitute the major portion of collagen and play an important role in human body. With increasing amounts of MBP, the amino acid content of the meat batters decreased, whereas the formulation with the lowest amount of MBP, MBP-10, was statistically similar to that of the control (21.0 g/100 g vs. 21.1 g/100 g). The amount of non-essential amino acids such as glycine and proline were significantly increased by approximately 43 and 21%, respectively, in meat batters with 40% MBP.” (Kakimov, 2017)

Calculated essential amino acid content in 100 g of protein in meat batter formulations; АS: Amino acid score, FAO: Food and agriculture organization of the united nations

“Notably, these two amino acids, along with the proline derivative oxyproline are the major constituents of collagen and have an important physiological role in that glycine participates in nitrogen metabolism and protein synthesis and also has a vital role in brain function. Meanwhile, proline is essential for muscle stamina, as proline deficiencies are associated with fatigue.” (Kakimov, 2017)

“Consumption of foods with high amino acid contents that can be used for collagen production will contribute to muscle development and regeneration. Overall, the essential amino acid content of meat batters prepared here conformed to the Food and Agriculture Organization of the United Nations (FAO) scale for ideal protein content (table above). However, in MBP-40 meat batters, the limiting amino acids were methionine and cysteine (amino acid score 97.3%) and tryptophan (AS 98.4%). Methionine is a major building block for proteins and is associated with vitamin B12 deficiency. Tryptophan boosts synthesis of the vitamin PP and deficiencies in this amino acid can lead to serious illnesses such as tuberculosis, cancer and diabetes.” (Kakimov, 2017)

“The highest amino acid score was seen for meat batters with 10% MBP. Increases in the amount of MBP were associated with decreasing amino acid scores (Table above). The highest amino acid score was calculated for lysine (175.96) in MBP-10 and this value decreased to 149.04 for MBP-40. Lysine is essential for bone formation and childhood development and also promotes calcium digestion and nitrogen metabolism in humans. Moreover, adequate lysine is critical for synthesis of antibodies and hormones as well as for collagen formation and tissue regeneration. The sum of the phenylalanine and tyrosine content for the control was around 50% higher than the FAO recommendation and the addition of MBP upto 40% decreased the value to a level that was closer to that of the FAO (Table Above).” (Kakimov, 2017)

“The approximate level of leucine and threonine in both the formation and the controls was higher than that of the FAO, although MBP-40 had the lowest amount. The MBP-40 also had the lowest amount of isoleucine relative to the control and was closest to the value set by the FAO (4.44 vs. 4.0). Isoleucine is essential for hemoglobin production and provides an energy source for muscle while also preventing early muscle fatigue. Threonine improves cardiovascular and immune system function and that of the liver. This amino acid is also involved in glycine and serine synthesis. Each of these amino acids is important for strengthening ligaments and all muscles, including the heart.” (Kakimov, 2017)

“Overall, these results indicate that the optimum quantity of MBP in meat batters ranges between 10 and 20% of total mass. Partial replacement of beef with a MBP can reduce production costs by as much as 15% while enriching meat batters with amino acids such as glycine, proline and oxyproline. However, excess amounts of MBP in meat batter formulations reduces their nutritive value and is inconsistent with regulations for meat products.” (Kakimov, 2017)


Beef and marrow barbecue in Argentinian way

These results are highly significant and show the scientific basis for the inclusion of bone meal in products intended for human consumption. We reviewed equipment available for producing bone meal. The Kakimov study is key in understanding the probably/ optimal range for inclusion of bone meal in fine emulsion meat products.

As far as equipment is concerned, this validates the work of Green Cell Technologies and their Dynamic Cell Disruption Technology which can accomplish what smaller equipment can do at a far increased rate and efficiency. They have demonstrated their equipment is able to reduce particle size of bones smaller and more effectively than other technology and since comminution of meat particles is tightly related to digestibility through greater bio availability (Notes on Comminution and Digestibility) for large plants this must remain their number one consideration. In many western countries, its inclusion in human food will remain problematic till legislative reforms are affected. Until such time, as far as bone meal is concerned, such technology’s main area of application will remain directed to the animal feed industry. Countries with greater sanity in legislation will have the opportunity to exploit technology like this to the direct benefit of their citizens through its inclusion into food for human consumption.

Further Reading

The End of the Rendering Plant

The Power of Microparticles: Disruptor (DCD) Technology

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Kakimov, A., Suychinov, A., Mayorov, A., Yessimbekov, Z., Okuskhanova, E., Kuderinova, N., and Bakiyeva, A.. (2017) Meat-bone Paste as an Ingredient for Meat Batter, Effect on Physicochemical Properties and Amino Acid Composition

Mohamed A. M. (2008). An overview of bone cells and their regulating factors of differentiation. The Malaysian journal of medical sciences : MJMS15(1), 4–12.

Paloheimo, L., Björkenheim, L. M., Leivonen, H.. (1965) STUDIES ON THE MAIN CHEMICAL COMPOSITION OF BONES, Department of Animal Husbandry, University of Helsinki,, Received January 2, 1965

Yessimbekov, Z., Kakimov, A., Caporaso, N., Suychinov, A., Kabdylzhar, B., Shariati, M. A., Baikadamova, A., Domínguez, R., Lorenzo, J. M.. 2021. Use of Meat-Bone Paste to Develop Calcium-Enriched Liver Pâté. Foods 2021, 10, 2042.

Photo Credit

All photos from

Collagen, Reticular and Elastic: A Closer Look

Collagen, Reticular and Elastic: A Closer Look
17 January 2022
Eben van Tonder

Dedicated to Dawie and Zelda


I’ve been working with animal parts high in collagen for the last few years, being bones, skin, tendons and organs. It is part of broader work aimed at using the complete animal and by-products for human food and animal feed, respectively. On the plant matter side, similar work is undertaken to use the entire plant to eliminate waste and achieve greater bioavailability from both for its functional role in food ingredients perspective as well as nutrition.

On 6 to 9 January 2022, I had an extremely productive weekend with Dawie Hyman and his twin sister Zelda at Boggomsbaai on the South African southern Cape coast. Inspired by them I decided to take a closer look at collagen to continue my investigation of skin/ hide/ tendons for an increased role in providing structure in Frankfurter style sausages both hot and cold. I dedicate this set of personal notes to Dawie and Zelda for their inspiration, motivation, and great friendship.

The structure of my investigation is based on the Ushiki (2002). These are my private notes to review the available scientific data which invariably leads to an application in food processing. I have been challenged to look at the role of collagen networks in providing structural support.

The overview of a few key papers written on the subject of extracellular networks and reviewing how collagen strands are formed in vitro and how the casings industry process collagen into edible casings, provided me with a completely new set of tools for further investigation into manipulating

One of my projects for 2022 will be focused on a production facility being set up in West Africa. Being back in such an environment is very exciting for me because it allows the slow progression of existing methods as opposed to the relentless pressure of a purely R&D environment where there is often unrealistic expectation of progress that must be turned into profit for the project to continue. I have been in such an environment for almost two years now. In contrast to this, a traditional meat processing plant’s first priority is to stick to time tested processes and incremental, almost unnoticeable changes. The relentless nature of the R&D environment taught me much and provided a firm basis for future work, but I believe this to be best done in a factory environment where such work is no more than 10% of daily tasks, giving ample time for careful thought and theoretical work before progressions are attempted.

When I had the opportunity to re-look the matter of bacon production, it was done in such an environment at Woodys Consumer Brands. Best Bacon and Rib System on Earth developed from this.

Apart from my own conclusions, reviewing the structures under discussion is rewarding, enriching and by itself provides great insight into the work of the meat/ plant processor. I prefer giving the interesting sections by quoting the authors verbatim allowing me the luxury of reviewing their work from time to time and discovering new elements for application that I have previously missed.

Philosophically, the work is very important to me as it goes to a fundamental requirement I have in meat and plant processing that it must be done with great respect as it involves the ending of life for the sake of survival. This is more obviously related to animals, but it is a faulty perspective that causes us not to see plants in the same light. Waste is an act of disrespect. Animal and plant waste is at the heart, I believe, of mainly Western disease. I made it a mission to investigate the entire animal carcass and the entire plant and find the great value that nature bestowed on every part of the animal and plant.

With these preliminary thoughts, let’s delve into the subject.

A. Relook at Collagen

Previous notes on collagen and gelatin I made are:

Collagen Marker: Hydroxyproline

Functional Value of Gelatin

Notes on Collagen

I looked at unprocessed beef tendons for inclusion in recipes:

Regarding Meals with Beef Tendons

Every application is in-line with the landmark work on meat emulsions which I feature in: Review of comminuted and cooked meat product properties from a sol, gel and polymer viewpoint

Most of the experimental work was done where I also considered Cell Disruption Technology:

The End of the Rendering Plant

The Power of Microparticles: Disruptor (DCD) Technology


“Collagen fibres present a cord- or tape-shaped 1-20 μm [10-6; millionth] wide and run a wavy course in tissues. These fibres consist of closely packed thin collagen fibrils (30-100 nm [10-9; billionth] thick in ordinary tissues of mammals), and exhibit splitting and joining in altering the number of the fibrils to form a three-dimensional network. Individual collagen fibrils (i.e., unit fibrils) in collagen fibres have a characteristic D-banding pattern whose length ranges from 64 to 67 nm [10-9; billionth], depending on tissues and organs. During fibrogenesis (mechanism of wound healing and repair), collagen fibrils are considered to be produced by fusing short and thin fibrils with tapered ends.” (Ushiki, 2002)

In vertebrates, there are 28 collagen types, and these are classified “according to domain structure, function and supramolecular assembly [for a review, see Mienaltowskiand Birk (2014)]. The most abundant are the fibrillar collagens that form the basis of the fibrils in bony, cartilaginous,fibrous and tubular structures.” (Kadler, 2017)

“Collagen fibrils are complex macromolecular assemblies that comprise different fibrillar collagen types (Hansen &Bruckner 2003). The fibrils are either ‘predominately type I collagen’ or ‘predominately type II collagen’. Predominatelytype I collagen fibrils occur in bony, tubular and fibrous tissues, whereas cartilaginous tissues contain predominately type II collagen fibrils. Collagen fibrils range in length from a few microns to centimetres (Craiget al.1989) and therefore have molecular weights in the tera Dalton range [based on calculations described by Chapman (1989)]. The fibrils provide attachment sites for a broad range of macro-molecules including fibronectin, proteoglycans and cell surface receptors such as integrins, discoidin domain-containing receptors and mannose receptors (Di Lulloet al.2002; Joki-nenet al.2004; Sweeneyet al.2008; Orgelet al.2011). Furthermore, the fibrils vary in diameter depending on species, tissue and stage of development (Parryet al.1978;Craiget al.1989) and in response to injury and repair (Pin-gelet al. 2014). Collagen fibrils are arranged in exquisite three-dimensional architectures in vivo including parallel bundles in tendon and ligament, orthogonal lattices in cornea, concentric weaves in bone and blood vessels and basketweaves in skin.” (Kadelr, 2017)

Reticular Fibres

“Reticular fibers are usually observed as a delicate meshwork of fine fibrils stained black by the silver impregnation method. They usually underlie the epithelium.” (Ushiki, 2002) “The epithelium is a type of body tissue that forms the covering on all internal and external surfaces of your body, lines body cavities and hollow organs and is the major tissue in glands.” (Cleveland Clinic)

“Epithelial tissue has a variety of functions depending on where it’s located in your body, including protection, secretion and absorption.

The organs in your body are composed of four basic types of tissue, including:

  • Epithelial.
  • Connective.
  • Muscular.
  • Nervous.

All substances that enter or leave an organ must cross the epithelial tissue first.

You have many different kinds of epithelial tissue throughout your body. Some examples of epithelial tissue include:

  • The outer layer of your skin (epidermis).
  • The lining of your intestines.
  • The lining of your respiratory tract.
  • The lining of your abdominal cavity.
  • Your sweat glands.”

(Cleveland Clinic)

Reticular fibres “cover the surface of such cells of muscle cells, adipose cells or fat cells, connective-tissue cells specialized to synthesize and contain large globules of fat and Schwann cells which are the main glial cells of the peripheral nervous system which wrap around axons of motor and sensory neurons to form the myelin sheath. “Electron-microscopically, reticular fibres are observed as individual collagen fibrils or a small bundle of the fibrils, although the diameter of the fibrils is thin (about 30 nm [10-9; billionth]) and uniform. Reticular fibres are continuous with collagen fibres through the exchange of these collagen fibrils. In silver-impregnated specimens, individual fibrils in reticular fibres are densely coated with coarse metal particles, probably due to the high content of glycoproteins around the fibrils.” (Ushiki, 2002)

Elastic Fibres

“Elastic fibres and laminae (a thin layer or scale of organic tissue) are composed of micro-fibrils and elastin components. Observations of the extracted elastin have revealed that elastin components are comprised of elastin fibrils about 0.1-0.2 μm [10-6; millionth] thick. Elastic fibres and laminae are continuous with networks and/or bundles of microfibrils (or oxytalan fibres) and form an elastic network specific to individual tissues.” (Ushiki, 2002)

Two Systems but Three Types

> Two Systems

“The fibrous components of the extracellular matrix are thereby morphologically categorized into two systems: 

a. the collagen fibrillar system (constituents of tendons) as a supporting framework of tissues and cells, and

b. the microfibril-elastin system for uniformly distributing stress to maintain the resilience adapted to local tissue requirements.” (Ushiki, 2002) “Fibrillin microfibrils are extensible polymers that endow connective tissues with long-range elasticity and have widespread distributions in both elastic and non-elastic tissues. They act as a template for elastin deposition during elastic fibre formation and are essential for maintaining the integrity of tissues such as blood vessels, lung, skin and ocular ligaments.” (Thomson, 2019)

> Three Types of Fibres

“Fibrous components of the extracellular matrix are classically divided into three types of fibres: collagen, reticular and elastic. This classification is based on the light microscopic findings (e.g., their shapes, staining properties and arrangements) and chemical properties of these fibres (e.g., MALL, 1896; FOOT, 1928; HAS, 1942); collagen fibres appear as thick and wavy strands stained pink with eosin, while reticular fibres are fine fibres stained dark with the silver impregnation method. Elastic fibres, on the other hand, are observed as a cord or sheet stained purple with resorcin-fuchsin or aldehyde-fuchsin staining, and are highly resistant to boiling water, in contrast with collagen fibres which are easily gelatinized in hot water.” (Ushiki, 2002)

“Electron microscopy has also revealed the ultrastructures of these fibrous components, namely that the collagen and reticular fibres are composed of fibrils with a unique banding pattern (ScHmirr et al., 1942), and elastic fibres comprise both fibrous and amorphous elements (GREENLEE et al., 1966). Advances in biochemistry and immunohistochemistry have also provided detailed information on the nature of these fibrous components, and a number of reviews are available, especially in consideration of the biochemical properties of the fibrous components (e.g., Ross, 1973; SANDBERG et al., 1981; KUHN, 1987; also see books edited by HAY, 1991; YURCHENCO et al., 1994)” (Ushiki, 2002)

>> Collagen

a. Collagen Fibres – Basic Structure

“Fresh collagen fibres are colourless strands 1 to 100 μm thick that usually follow a wavy course without branching in tissues. These fibres are stained pink with eosin and green with the Masson trichrome staining method (Fig. la).” (Ushiki, 2002)

“Electron microscopy shows collagen fibres to be a bundle of closely packed thin fibrils with periodical cross striations (SCHMITT et al., 1942) (Fig. lb, c); these unit fibrils are called “collagen fibrils.” ” (Ushiki, 2002)

“In specimens stained with a cationic dye such as Alcian blue and Cupromeronic blue, very thin filaments (less than 10 nm thick) are visible within the bundle of collagen fibrils (Fig. Id) (Scum’, 1980, 1988, 1995; SCOTT and ORFORD, 1981; RUGGERI and BENAZZO, 1984, RASPANTI et al., 2002). These filamentous structures have been considered proteoglycans, including large dermatan sulfate proteoglycans and such small molecules as decorin (FLEISCHMAJER et al., 1991). The proteoglycan filaments appear to connect neighbouring collagen fibrils by transversely and periodically attaching to a specific site of the fibrils.” (Ushiki, 2002)

“These findings indicate that proteoglycans play a role in synchronizing the position of bands in neighbouring fibrils and determine the distance of two neighbouring fibrils to fasten themselves into a bundle.” (Ushiki, 2002)

“Thus, the structure of collagen fibres in which parallel fibrils are bundled with flexible proteoglycans is in accordance with their mechanical properties, since collagen fibres are flexible but offer great resistance to a pulling force.” (Ushiki, 2002)

Fig. 1. Collagen fibres observed by light microscopy (a), TEM (b) and SEM (c, d). a. Collagen fibres in the dermis in the human skin. These fibres are stained pink with hematoxylin-eosin and run in various directions. x 200.
b. Longitudinal section of a collagen fibre in the dermis of the human skin. The light-microscopically determined collagen fibre is a bundle of collagen fibrils. Note single fibrils (arrowheads) running independently from the bundle. x 21,000. c. SEM image showing the three-dimensional structure of the collagen fibre in the mouse peritendineum (any of the fibrous sheaths surrounding the primary bundles of fibres in a tendon). The collagen fibre is observed as a bundle of closely packed collagen fibrils with characteristic transverse hands. x 62,000 (Bar=100 nm). d. Closer view of a collagen bundle in the rat aortic adventitia, which has been treated with a 2% glutaraldehyde solution containing 0.05% Aldan blue and 0.3 M MgCL (0.025 acetate buffer, pH, 5.8). Thin filamentous structures (arrowheads) appear to connect neighbouring collagen fibrils by attaching transversely and periodically to a specific site of collagen fibrils. x 155,000 (Bar =100 nm)

b. Collagen Fibres – Arrangement

“The size and shape of collagen fibres (i.e., bundles of collagen fibrils) vary depending on tissues and organs, even within the same species. They are usually of a cord- or tape-shape with a width of 1-20 μm, and take a wavy course (Fig. 2a, b), even if they form dense fibrous connective tissues such as the tendon (ROwE, 1985). The wavy arrangement of these fibres probably provides resilience to the fibres themselves, which also serves as a cushion against the direct tension to collagen fibres.” (Ushiki, 2002)

“In loose connective tissues, collagen bundles sometimes run parallel to each other to be twined into a larger bundle, while they come to split and join by changing the number of collagen fibrils, thus forming a three-dimensional meshwork throughout the tissues. Much thinner fibres also often participate in the collagen fibre network (ORBERG et al., 1982; USHIKI and IDE, 1990); these fibres are composed of single or several collagen fibrils, which are produced by leaving the thicker fibers to rejoin them in another portion. This fibrillar network is similar to the network formed by reticular fibres, but does not have argyrophilic  properties (i.e. do not readily stained black by silver salts).” (Ushiki, 2002)

This fibrillar network probably plays a role in maintaining a specific arrangement of collagen fibres in each tissue and organ.

Fig. 2. The shape and arrangements of collagen fibers observed by SEM. a. Cord-shaped collagen fibers entangled in the human subcutaneous tissue (Subcutaneous tissue is the deepest layer of your skin. It’s made up mostly of fat cells and connective tissue. The majority of your body fat is stored here). x 1,700 (Bar =5 μm). b. Tape-shaped collagen fibers in the rat aortic adventitia. Much thinner bundles or single collagen fibrils (arrowheads) leaving thick bundles form a loose net around collagen bundles. x 2,200

c. Collagen Fibres – Structure of the collagen fibrils

“As described above, collagen fibrils are unit fibrils which can be observed in individual collagen fibers by electron microscopy (Fig. 3a, b). These fibrils are cylindrical in shape with a diameter ranging from 10 to over 500 nm (mean diameter about 40-80 nm) in mammals (PARRY and CRAIG, 1984). They show periodical striations (which are alphabetically named the A-E bands) in positively stained sections (ScHmiTT and GROSS, 1948; BRUNS and GROSS, 1974), while the characteristic alternation of dark and light zones is found along the negatively stained fibrils by TEM (TROMANS et al., 1963, OLSEN, 1963). The periodicity of these structures is determined by the length of the two closest D-bands in positively stained fibrils and called D-periodicity. The surface morphology of the collagen fibrils has also been studied by TEM of shadowed materials (GROSS and SCHMITT, 1948) and freeze-fractured replica (MARCHINI and RUGGERI, 1984; RASPANTI et al., 1989), SEM (RASPANTI et al., 1996) and AFM (Fig. 3c, d) (BASELY et al., 1993; USHIKI et al., 1996; YAMAMOTO et al., 1997). These studies revealed the presence of periodical grooves and ridges on the surface of collagen fibrils, which correspond to dark and light zones of negatively stained fibrils, respectively.” (Ushiki, 2002)

Numbers of studies have been devoted to the arrangement of collagen molecules in each fibril (e.g., see review of CHAPMAN and HULMES, 1984). They established that the periodic structure in collagen fibrils arises because the molecules about 300 nm long are assembled in parallel array and are mutually staggered by integral multiples of a D-period. The D periodicity has been estimated by electron microscopy and low-angle X-ray diffraction methods. Low angle X-ray diffraction of collagen fibrils showed that D is close to 67 nm in wet samples, and around 64 nm in air-dried samples (BEAR, 1944; BRODSKY and EIKENBERRY, 1982). By electron microscopy, D varies from 64-70 nm in ultrathin sections, and the variability has been interpreted as the effect of various degrees of shrinkage caused by the dehydration and embedment of samples. In contrast, some authors claim that the D-periodicity differs among collagen fibrils in different organs; for example, the D-periodicity of bovine corneal collagen fibrils was reported by X-ray diffraction to be shorter than that of rat tail tendon collagen fibrils (MARcBINI, et al., 1986).” (Ushiki, 2002)

“On the other hand, the presence of subfibrils in collagen fibrils has been reported by previous investigators using TEM of such samples as glycerinated or denatured tissues (Fig. 4a) (e.g., BOUTEILLE and PEASE, 1971; RAYNS, 1974; LILLIE et al., 1977). These studies indicate that right-turning subfibrils are tightly packed in individual collagen fibrils. RUGGERI et al. (1979) also noticed that the subfibrils have a straight or helicoidal arrangement depending on the types of tissue located.  Ushiki (2002) investigated collagen fibrils of the cornea and sclera by AFM, and found a difference in D-periodicity between corneal and scleral fibrils in relation to the inclination angle of the subfibrils  (YAMAMOTO et al., 2000a). More precisely, the corneal collagen fibrils (with a D-periodicity of 63 nm) show a helicoidal arrangement of right-turning subfibrils with a 15° spiral angle, while subfibrils in the scleral collagen fibrils (with a periodicity of 67 nm) run almost longitudinally along the fibrillar axis. The relationship between these subfibrils and collagen molecules is still an open question (CHAPN4AN and HULMES, 1984), although several authors consider the subfibrils to be aggregations of small numbers of collagen molecules (VEis, et al., 1967; SMITH, 1968; BOUTEILLE and PEASE, 1971).” (Ushiki, 2002)

Fig. 3. Collagen fibrils observed by TEM (a, b) and AFM (c, d). a. Collagen fibril (in the mouse tail tendon) stained positively with uranyl acetate and lead citrate. The fibril shows periodical striations with an identity period of about 67 nm. Arrowheads indicate d-bands.  x 105,000. b. Collagen fibril (in the mouse tail tendon) stained negatively with phosphotungstic acid. The characteristic alternation of dark and light zones is found along the fibrils. x 105,000. c. AFM image of a bovine scleral collagen fibril. The fibril has periodical transvers grooves and ridges. Shallow longitudinal grooves are also found on the surface of collagen fibrils. d. The longitudinal section profile of the scleral collagen fibril between two asterisks in c. The height as well as the width of each portion can be measured from this profile. (Fig. 3a and b are from Mr. S. HAYASHI, Iwate Medical University. Fig. 3c and d are reproduced from YAMAMOTO et al., 2000a with permission).

“The diameter of collagen fibrils varies from 10-500 nm, depending on the locations of the tissues as well as the age and species of animal (PARRY and CRAIG, 1984). For example, the cornea has collagen fibrils with a regular diameter of about 30 nm, while the diameter of scleral collagen fibrils variously ranges from 25-230 nm (KomAi and USHIKI, 1991, YAMAMOTO et al.,1997). Collagen fibrils in tendons and ligaments show differing diameters with a peak one of 100-200 nm (PARRY et al., 1978). Another example is the diameter of collagen fibrils in the peripheral nerves (UsHIKI and IDE, 1990), where fibrils are thicker in the epineurium than in the endoneurium in various mammals (Fig. 4d). What determines the shape and size of collagen fibrils is an interesting question. Some investigators believe that the copolymeration of collagen molecules with other components of the extracellular matrix may influence the diameter of the fibrils formed (see review of CHAPMAN, 1989), while others have stated the importance of the copolymerization of different kinds of collagen molecules in one fibril (LAPIERE et al., 1977, FLEISCHMAJER et al., 1985, also see review of PROCKOP and HULNIES, 1994).” (Ushiki, 2002)

d. Collagen Fibres – Collagen molecule and its assembly

Fig. 4 a. SEM view of collagen fibrils (of the mouse tail tendon) treated with 8 M urea in a 0.2 M Tris-HCI buffer for 30 min. Longitudinal clefts are found in the individual fibrils, suggesting the dissociation of subfibrils. D-banding is still preserved in the denatured fibrils.  x 49,500 (Bar =100 nm). b. Collagen type I molecules observed by AFM. This molecule is observed as flexible thread 300 nm long. Globular bulges are present at both ends of the molecule. x 192,000 (Bar = 50 nm). c. Procollagen I molecules observed by AFM. Arrowhead indicates a globular C-terminal propeptide. (This sample was kindly provided by Dr. Fumio NAKAMURA, Hokkaido University) x 150,000 (Bar =50 nm). d. TEM view of a transverse section of connective tissue sheath in the rat sciatic nerve. This section comprises the whole thickness from the epineurium (Ep), through the perineurium (P) to the endoneurium (En). The diameter of the collagen fibrils is 30-100 nm in the epineurium, 30-60 nm in the perineurium and 40-45 nm in the endoneurium. x 16,500 (Bar= 1 gm)

“Chemical studies have revealed that the type I, II, and III collagen molecules self-assemble into banded fibrils. The shape of these collagen molecules has been studied previously by TEM using shadowing techniques (e.g., SILVER and BIRK, 1984; see also a book edited by MAYNE and BURGESON, 1987), and recently by AFM (SHATTUCK et al., 1994; LIN et al., 1999; YAMAMOTO et al., 2000b). As for the type I molecules, they are thin and flexible threads about 300 nm in length in contrast with type I procollagen molecules with a globular C-terminal propeptide and fuzzy N-terminal propeptide in either end (Fig. 4h, c). The individual collagen fibrils are generally considered to be formed from collagen molecules by their self-assembly process in the extracellular environment (BIRK et al., 1995; KADLER et al., 1996). Our SEM studies showed a process of collagen fibril assembly in cultures of human osteosarcoma cells (HASHIZUME et al., 1999); the findings clearly showed that short and thin collagen fibrils (about 1 μm long and 30 nm thick) with tapered ends fused with each other in a helical direction with their periodicity synchronized with each other, forming longer and thicker collagen fibrils. During this process, the banding pattern from end to end in the fibrils is unidirectional, indicating that  the  directions of the collagen molecules are uniform  throughout  the  length  of  the  individual fibrils.” (Ushiki, 2002)


“Basic structure of reticular fibers in relation to their staining properties. Reticular fibers are fine fibers forming an extensive network in certain organs. By light microscopy, these fibers are not visible in conventional stains such as hematoxylin and eosin, but are stained dark with a silver impregnation method (Fig. 5a) (MALLORY and PARKER, 1927; FOOT, 1928; NAGEOTTE and GUYON 1930). Thus, reticular fibers are also called argyrophilic fibers. The distribution of reticular fibers is rather restricted: they are usually found mainly in the basement of epithelial tissues, the surface of adipose cells, muscle cells and Schwann cells, outside the endothelium of the hepatic sinusoid, and the fibrous reticulum of lymphoid tissues. These fibers have a diameter of less than 2 μm. Although there are several modifications of BinscHowsKY’s impregnation method (MAREscH, 1905), a method reported by IsHII and ISHII (1965) yields specimens with suitable representation showing the fine structure of reticular fibers. In these specimens, reticular fibers are meshworks of very fine, dark fibrils, and are continuous with thin and reddish collagen fibers (Fig. 5a).” (Ushiki, 2002)

Fig. 5. Reticular fibers obserbed by light microscopy (a) and electron microscopy (b-e). a. Reticular fibers of the human lingual muscle stained by a modification of Bielschowsky’s impregnation method of Ism and Isliff (1965). Reticular fibers are observed as a meshwork of very fine, dark fibrils, which surrounds the muscle fiber as the endomysial sheath. Note reddish collagen fibers continuous with the dark reticular fibers of the endomysial sheath. x 1,500. b. Reticular fibers surrounding a rat lingual muscle fiber. Thin collagen fibrils and their small bundles are tightly attached to the basal lamina of the muscle fiber. x 8,500. c. TEM view of a silver impregnated section of the dog lingual muscle. The reticular fibers are composed of a bundle of argyrophilic fibrils attached to the basal lamina of skeletal muscle fiber. x 14,000. d. Backscattered electron (BSE) image of the reticular fibers of the human hepatic sinusoid by SEM. Because the BSE yield strongly depends on the average atomic number of structures (UsHixi and FUJITA, 1986), metal particles are clearly visualized as highlights in this micrograph. Thus, it is clear that the individual fibrils of the reticular fibers are densely coated with coarse metal particles. x 33,000. e. BSE image of a collagen fiber of the interlobular connective tissue in the human liver. Fine metal grains are sparsely deposited on the surface of the collagen fibrils. x 33,000 (Specimens of Fig. 3a, c-e were kindly provided by Prof. emer. T. ISHII, Tohoku University)

“Electron microscopy shows reticular fibers as individual collagen fibrils or a small bundle of collagen fibrils (Fig. 5h). These collagen fibrils have striations with a characteristic D-banding pattern similar to fibrils in collagen fibers, but their diameter is rather thin and uniform, ranging from 20-40 nm. Observations of silver-impregnated sections by TEM and SEMI (using backscattered imaging) show that individual collagen fibrils in reticular fibers are densely coated with coarse metal particles, while fine granular particles are sparsely found on fibrils in collagen fibres (Fig. 5c-e) (ScHwARTz, 1953; USHIKI, 1992b). This indicates that the size and density of metal precipitation particles determine the difference in tone between reticular fibers and collagen fibrils light-microscopically.” (Ushiki, 2002)

“Reticular fibers are also PAS-positive and have an affinity to cationic stains such as Ruthenium Red (IDE et al., 1989). These findings suggest that the surface of the individual fibrils in reticular fibers is embedded in an abundance of glycoproteins, which produce the stainability of fibers described above.” (Ushiki, 2002)

“Chemical and immunohistochemical studies, on the other hand, have revealed that reticular fibers, in contrast to collagen fibers composed of collagen type I, comprise mainly collagen type III (FLEISCHIVIAJER et al., 1980; MONTES et al., 1980) in association with other types of collagen (e.g., collagen type V), glycoproteins (STENNIAN and VAHERI, 1978), and proteoglycans/ glycosaminoglycans (MONTES et al., 1980; NISHIMURA et al., 1996). The difference in collagen type between collagen fibers and reticular fibers might be related to the diameter of the fibrils in the two fibers, although further studies will be needed in this point.” (Ushiki, 2002)

Fig. 6. SEM views of reticular fibres in specimens treated with an alkali-water maceration method by 011TANI (1987). In these specimens, cellular elements, elastic fibres and basal laminae are completely removed without any severe damage to the collagen fibrils of reticular fibres. a. Endomysial reticular fibres (R) of the dog lingual muscle. The space for accommodating the skeletal muscle fibre is demarcated by a cylindrical sheath of reticular fibres. Note the thicker collagen bundle (or collagen fibres, C) following a wavy course outside the endomysial sheath. x 1,200. b. Closer view of a part of Figure 6a. The sheath of reticular fibres consists of thin collagen fibrils, which are elaborately interwoven into delicate patterns of lacework. x 4,200. c. Reticular fibers in the deep cortex of the rat mesenteric lymph node. Because the cellular elements such as reticular cells and lymphocytes were removed by the maceration method, the three-dimensional network of reticular fibers can be directly observed by SEM. B the reticular sheath for blood vessels.  x 570, d. Closer view of the sheath of reticular fibers for blood vessels in the same specimen of Figure 6c. This sheath is observed as a lacework of thin collagen fibrils. Arrow indicates that portion where collagen fibrils in this sheath are continuous with thicker bundles of collagen fibrils as a reticular framework of the lymphoid tissue. x 1,400

a. Reticular Fibers – Arrangement

“The arrangement of reticular fibers is important for understanding the functional role of the fibers in tissues and organs, and was first studies mainly by light microscopy (PLENK, 1927; NAGEOTTE and GUYON, 1930). SEM further revealed the threedimensional architecture of reticular fibers in relation to the surrounding components (e. g., MOTTA, 1975; SAWADA 1981; USHIKI and IDE, 1986). The method introduced by OHTANI (1987) is also useful for visualizing the fibrillar arrangement more directly and precisely by SEM, since it successfully removes cellular elements, elastic fibers, and basal laminae without any severe damage to the collagen fibrils.” (Ushiki, 2002)

“These findings show that reticular fibers form a delicate network of fine fibrils which underlie the basal lamina of such cells as epithelial, muscle and Schwann cells (OHTANI, 198.8, OHTANI et al, 1988, 1991, USHIKI and IDE, 1990, MURAKUMO et al., 1993). The firm attachment of the individual fibrils with the basal lamina indicates that the collagen fibril meshwork and the basal lamina, as a whole, form a distinct structural unit for the demarcation and support of cellular components (USHIKI and IDE, 1986; USHIKI et al., 1990).” (Ushiki, 2002)

“The reticular arrangement of the fibrils is also suitable for providing a space for molecular movement in the extracellular fluid. Concerning lymphoid tissues, reticular fibers act as a skeletal framework and support vessels and lymphatic sinuses within the tissues (USHIKI et al., 1995).” (Ushiki, 2002)

“Reticular fibers thus differ in structure, arrangement,  and function from collagen fibrils, but are continuous with collagen fibers. In this sense, the two fibrous components are considered to form an extensive network of collagen fibrils as the collagen fibrillar system (USHIKI, 1992b).” (Ushiki, 2002)

>> Elastic Fibres

“Elastic tissues of the body owe their mechanical properties to the protein elastin. In complete contrast to the highly orientated, inextensible collagen fibre the elastin fibre occurs naturally in a contracted state and is capable of reversible extension to about double its length. Elastin is therefore generally found in the form of fibres. It is also found as membranes in the elastic ligaments, elastic blood vessels, and other compliant tissues such as lung and skin. The elastic arteries contain concentric layers of elastic fibres, and the ligaments have parallel fibres (Partridge, 1962).” (Bailey, 1878)

“Elastin was at first defined solely by its histological appearance. Largely through the work of Partridge and his colleagues, a precise chemical definition of elastin was reported in 1958. However, it was not until the cross-links were identified by this group in 1963 (Thomas et al., 1963) that the field opened up and a significant understanding of the relationship of structure to function began to emerge.” (Bailey, 1978)

“Like collagen, elastin is an extracellular insoluble polymeric protein; hence its intracellular biosynthesis as a soluble monomer, its extracellular aggregation and subsequent stabilisation by crosslinking considerably resemble the biosynthesis of collagen fibres.” (Bailey, 1978)

Fig. 7. Elastic fibers observed by light microscopy (a) and TEM (b, c). a. Elastic fibers in the stretch preparation of the rat subcutaneous tissues stained with aldehyde-fuchsin and light-green. Elastic fibers are stained violet with aldehyde-fuchsin, while collagen fibers are observed green by light-green staining. x 125. b. TEM view of elastic fibers in the section stained with uranyl acetate and lead citrate. The elastic fiber is composed of an amorphous substance (or elastin, E) and microfibrils (arrowheads). x 77,000. c. Transverse sectoin of an elastic fiber stained with tannic acid and lead citrate. Elastin of the elastic fibers is stained dark in this micrograph. Arrows indicate collagen fibrils. x 65,000

a. Elastic Fibres – Basic Structure

“Elastic fibers are generally twisted or straight strands stained by a resorcin-fuchsin or aldehyde-fuchsin method (Fig. 7a); these fibers are about 0.2 – 1.5 μm and sometimes branch to form a coarse network in loose connective tissues. In dense elastic tissues such as the aorta, elastic fibers fuse to form flattened sheets, or elastic laminae. Biochemically, elastic fibers are highly resistant to boiling water, in contrast with collagen fibrils which are easily gelatinized in hot water (RICHARDS and GIES, 1902).” (Ushiki, 2002)

“By TEM of ultrathin sections stained with uranyl acetate and lead citerate, elastic fibers are seen to consist of amorphous and fibrous components (Fig. 7b) (GREENLEE et al., 1966; Ross and BORNSTEIN, 1969). Amorphous components are densely stained with tannic acid treatment by TEM (Fig. 7c) (MIZUHIRA and FUTAESAKU, 1972) and are composed of substances which can be purified in boiling water and are recognized biochemically as the protein named elastin (e. g., see a review of Ross, 1973). Elastin endows elastic fibers with the characteristic property of elastic recoil. Fibrous components, on the other hand, correspond to the microfibrils which were recognized by TEM in various tissues and organs by Low (1962). Microfibrils are 10 nm in diameter and composed of various glycoproteins, including fibrillin (SAKAI, et al., 1986) and the amyloid P component (INouE and LEBLOND, 1986; INOUE et al., 1986).” (Ushiki, 2002)

“By conventional SEM, elastic fibers are observed as cobwebbed cords entangled with microfibrils (Figs. 8a, b, 11b) (USHIKI, 1992b).” (Ushiki, 2002)

Fig. 8. SEM images of elastic fibers (a, b) and elastin components (c, d). a. Elastic fibers (E) in the mouse aortic adventitia. Elastic fibers are observed as coiled or straight cords entangled in the net of microfibrils. C collagen fiber. x 9,100. b. Closer view of an elastic fiber (in the mouse subcutaneous tissue). The elastic fiber is covered densely with microfibrils which run in various directions.  x 55,000. c. Elastin components of the rat aortic adventitia treated with the formic acid-digestion mothod (UsHiiti, 1992a). This method removes cellular components, collagen components and microfibrils from tissues, while leaving elastin components unchanged at their original locations. Elastin fibers in this micrograph are observed as cords running in various directions. Note a connection between two crossed fibers (arrow). x 5,500. d. Internal elastic lamina of the rat aorta treated with the formic acid-digestion method. The lamina appears as a solid sheet with two large fenestrations. The surface of the lamina is somewhat fibrous. Fibrous structures are also found in the fenestrations where the fibrils extending the lamina to form a meshwork like a wire fence. x 3,000.

b. Elastin Fibres – Arrangement

“Since elastic fibres are intermingled with collagen fibrils and cellular elements in tissues, it is usually difficult to demonstrate their arrangement both extensively and three-dimensionally. For this reason, previous SEM investigators have attempted to extract elastic fibres by autoclaving tissues (GRu’r et al., 1977), or by utilizing treatments with chemical agents and enzymes: e.g., guanizinium chloride, collagenase, sodium hydroxide, and formic acid (KUHN, 1974; KEWLEY et al., 1977; WASANO and YAMAMOTO, 1983; SONG and ROACH, 1985; CRISSMAN, 1987). These methods selectively remove non-elastin components including microfibrils, collagen fibrils and cellular elements, and are effective for observing the architecture of elastin components in tissues by SEM (Figs. 8c, d, 9c, d). On the other hand, the treatment of tissues with a KOH method is effective for observing the special relationship between elastin components and cellular elements by SEM, since this method removes collagen fibrils and basal laminae while leaving cellular and elastin elements unchanged at their original shapes and locations (Fig. 9a, b) (USHIKI and MURAKUMO, 1991).” (Ushiki, 2002)

“Through these studies, several investigators have demonstrated that elastin components form a continuous network or sheet with a smooth surface (KuHN, 1974; WASANO and YAMAMOTO, 1983), while others have considered them as a fibrous network or sheet composed of fibrils about 0.1-0.2 μm (KEWLEY et al., 1977; HART et al., 1978). Our previous studies revealed that the surface structure and organization of elastin components are changeable depending on the procedures after extraction, and yielded evidence that the elastin component including aortic laminae are fibrous when extracted tissues are adequately treated (UsHIKI and MURAKUMO, 1991; USHIKI, 1992a).” (Ushiki, 2002)

“Elastin components show morphological features specific to individual tissues and organs (UsHIKI and MURAKUMO, 1991). A typical organization of elastin fibers in the loose connective tissue is a loose network of elastin fibers about 0.2-1.5 μm thick (Fig. 8c). An elastin sheet lining the serosal covering of the mesothelium consists of fine fibers ranging from 0.1- 1.0 μm thick, which run in various directions two-dimensionally and are elaborately interwoven, forming a delicate lacework-pattern (Fig. 9a, b). Elastic laminae in the aorta appear as a solid sheet about 2 μm thick with numerous oval fenestrations of varying diameters from 1-10 μm (Figs. 8d, 9d).  These laminae appear to be composed of fibrous structures about 0.1-0.2 μm thick. It is therefore evident that extracted elastin components are basically composed of thinner fibrils about 0.1-0.2 μm thick (Fig. 9h), even though some investigators further recognized very thin (3-4 nm thick) elastin filaments by TEM of negative-stained or freeze-etched specimens (GOTTE et al., 1974; FORNIERI et al., 1982). The elastin fibrils are present individually or in bundles, and so form elastin fibrils, fibers and/or laminae in individual tissues (Fig. 10) (UsHIKI and MURAKUMO, 1991).” (Ushiki, 2002)

“The organization of elastin fibers and laminae apparently influences the resilience of tissues suitable for their mechanical properties. Concentric elastic laminae with connecting interlaminar fibers are suitable for distributing blood pressure uniformly and effectively to the vascular wall. The elastic sheet lining the mesothelium is believed to give elasticity to the serous membrane and protect the mesothelium against any distention and contraction of such organs as the lung and urinary bladder.” (Ushiki, 2002)

Fig. 9. SEM images of elastin components after KOH (a, b) or formic acid (c, d) treatmemt. a. Elastin observed in the serosa of the mouse urinary bladder. The mesothelium (M) is removed in the lower right of the micrograph, where elastin forms a delicate pattern of lacework. x 1,300. b. Closer view of the elastin network in the serosa. The network is composed of fine elastin fibers and fibrils, which run in varoius directions and are elaborately interwoven. x 2,500. c. High magnification of an elastin fiber in the adventitia. The elastic fiber is seen as a bundle of fine fibrils about 0.1-0.2 μm. x 15,000. d. Part of transverse section of the rat aortic media. The medical elastic laminae and interlaminar elastin fibers are observed. x 1,500 (Fig. 9a is reproduced from USHIKI and MURAKUMO, 1991 with permission)

> Microfibril-elastin network system

“Microfibrils are usually present in and around elastin fibers, where they appear to be arranged in random directions to the elastin fibers (Fig. 8b) 1992b). In stretched fibers, the microfibrils change in their direction along the fibers, in response to stretching of the elastin fibers.  Microfibrils often leave elastin fibers to form a bundle or cobwebby meshwork in various tissues (Figs. 8a, 11b).” (Ushiki, 2002)

Fig. 10. Schematic drawing of elastin components. Elastin components are basically composed of unit fibrils about 0.1-0.2 μm thick. These elastin fibrils are present individually or in bundles to form elastin fibers, an elastin meshwork and/or elastin sheet in tissues.
Fig. 11 a. Light micrograph of the mouse subcutaneous tissue stained with aldehyde-fuchsin after oxidation with peracetic acid. Oxytalan fibers run in various direction like a cobweb throughout the tissue. Arrowheads indicate elastin fibers. x 50. b. SEM view of a part of the rat aortic adventitia. Microfibrils leave the elastic fiber (E) to form a bundle of microfibrils (0), which corresponds light-microscopically to the oxytallan fiber. C collagen fiber. x 11,000

“Light-microscopically, characterized fibrous structures are observed when sections are treated with peracetic acid before aldehyde-fuchsin staining (Fig. 11a) (FunmER and LILLIE, 1958). These fibrous structures are continuous with clastic fibres and are called oxytalan fibres. By TEM, the oxytalan fibres are observed as a bundle of microfibrils (Fig. 11b) (COTTA-PEREIRA et al., 1976). The oxytalan fibres can be also found in the zonule fibres of the eye and in the dermis where it connects the elastic fibres to the basal lamina. As far lymphatic vessels, oxytalan fibres act as anchoring fibres which connect the elastic fibres and lymphatic endothelium, thus preventing the collapse of initial lymphatics in tissues (Gum et al., 1990). In addition, so-called elaunin fibres (GAw-LIK, 1965) have intermediate characteristics between oxytalan fibres and elastic fibres by TEM (COTTA-PEREIRA et al., 1976). These findings indicate that microfibrils and  elastin  fibrils  produce  oxytalan fibres, elaunin fibres, and elastic fibres to form, as a whole, the microfibril-elastin fibre system which plays a role in maintaining the resilience adapted to local tissue requirements.” (Ushiki, 2002)

> Fibrillar System

What is the fibrilar system? Fibrils are structural biological materials found in nearly all living organisms. It differs from fibres which are longer than it is wide and filaments which are long-chain protein monomers as found in muscles and hair. Fibrils tend to have diameters ranging from 10-100 nanometers (whereas fibres are micro to milli-scale structures and filaments have diameters approximately 10-50 nanometers in size). Fibrils are not usually found alone but rather are parts of greater hierarchical structures commonly found in biological systems.

Wikipedia elaborates on the structure and mechanics of fibrils as follows. They “are composed of linear biopolymers and are characterized by rod-like structures with high length-to-diameter ratios.

Visualise length to diameter ratios. The bigger the number, the longer the strand. (Image from US Neodymium Magnets)

“They often spontaneously arrange into helical structures. In biomechanics problems, fibrils can be characterized as classical beams with a roughly circular cross-sectional area on the nanometer scale. As such, simple beam bending equations can be applied to calculate flexural strength of fibrils under ultra-low loading conditions. Like most biopolymers, stress-strain relationships of fibrils tend to show a characteristic toe-heel region before a linear, elastic region. Unlike biopolymers, fibrils do not behave like homogeneous materials, as yield strength has been shown to vary with volume, indicating structural dependencies. Hydration has been shown to produce a noticeable effect in the mechanical properties of fibrillar materials. The presence of water has been shown to decrease the stiffness of collagen fibrils, as well as increase their rate of stress relaxation and strength. From a biological standpoint, water content acts as a toughening mechanism for fibril structures, allowing for higher energy absorption and greater straining capabilities.

Fibrils mechanical strengthening properties originate at the molecular level. The forces distributed in the fiber are tensile load carried by the fibril and shear forces felt due to interaction with other fibril molecules. The fracture strength of individual collagen molecules is as a result controlled by covalent chemistry between molecules. The shear strength between two collagen molecules is controlled by weak dispersive and hydrogen bond interactions and by some molecular covalent crosslinks. Slip in the system occur when these intermolecular bonds face an applied stress greater than their interaction strength.”

“Intermolecular bonds breaking do not immediately lead to failure, in contrast they play an essential role in energy dissipation that lower the stress felt overall by the material and enable it to withstand fracture.  These bonds, often hydrogen bonding and dispersive Van der Waals interactions, act as “sacrificial” bonds, existing for the purpose of lowering stress in the network. Molecular covalent crosslinks also play a key role in the formation of fibril networks. While crosslinking molecules can lead to strong structures, too much crosslinking in biopolymer networks are more likely to fracture as the network is not able to dissipate the energy, leading to a material that is strong but not tough. This is observed in dehydrated or aged collagen, explaining why with age human tissues become more brittle.

> Fibrilogenesis

I quote two interesting comments from Gross (1958).

“Factors which may regulate the rate of fibril formation in systems in vitro are of interest from a physiological viewpoint for the clues they may give concerning mechanisms in viva, and from a physical chemical point of view for the light, they may shed on intermolecular reactions. Collagen soluble in cold neutral salt solutions has the interesting property of precipitating, on warming to body temperature,
as a rigid gel composed of fibrils with the characteristic axial periodicity of native collagen. It has been postulated that fibrils are formed under similar conditions in the extracellular tissues by spontaneous polymerization of collagen molecules secreted by the fibroblast into the ground substance.” (Gross, 1958)

In their paper Gross and Kirks (1958) describe some of the environmental factors which can influence the rate of fibril formation in neutral solutions of collagen. I made the paper available for download in the reference section below.

In their summary, they list the accelerators of fibril formation being SCN-, HCOB-, I-, Br-, F-, Cl-, in that order of effectiveness as measured by their relative ability to reverse the inhibitory effect of urea. Lysine
and Li+ were also strong accelerators of gelation.

Karl Kadler did a mini review of collagen fibrillogenesis in response to him receiving the Fell Muir Prize for 2016 by the British Societyof Matrix Biology. I have his article available for download in the referense section.

Fibrillogenesis “is the process by which triple helical collagen molecules assemble intocentimetre-long fibrils in the extracellular matrix of animals. The fibrils appeared abillion years ago at the dawn of multicellular animal life as the primary scaffold fortissue morphogenesis. The fibrils occur in exquisite three-dimensional architecturesthat match the physical demands of tissues, for example orthogonal lattices in cornea, basket weaves in skin and blood vessels, and parallel bundles in tendon, ligament and nerves.” (Kadler, 2016)

“Creating collagen vibrils in vitro is of the greatest interest for our study. Kadler refers to the work of Gross and mentions other researchers when he writes, “Gross (Gross & Kirk 1958), Wood & Keech (Wood & Keech 1960), Hodge & Petruska (Hodge 1989), Silver (Silver & Trelstad 1980) and Chapman (Bard & Chapman 1968), to name a few, showed that exposure of animal tissues (typically skin and tendon) to weak acidic solutions (typically acetic acid) or neutral salt buffers yielded a solution of collagen molecules that when neutralized and warmed to approximately 30°C, produced elongated fibrils that had the same alternating light and dark transmission electron microscope banding appearance as fibrils occurring in vivo (Holmes & Chapman 1979).” (Kadler, 2016)

“The characteristic banding pattern of the fibrils arises from D-stagger-ing of triple-helical collagen molecules that are 4.49Dinlength (where D is 67 nm, to a close approximation). The electron-dense stain used at neutral pH penetrates more readily into regions of least protein packing (the ‘gaps’) between the N- and C-termini of collagen molecules that are aligned head-to-tail along the long axis of the fibril. The fact that fibrils with D-periodic banding could be formed in vitro from purified collagen showed that all the information required to form a collagen fibril was contained within the amino acid sequence and triple helical structure of the collagen molecule (Hulmeset al.1973).” (Kadler, 2016)

> Elastogenesis

Fig. 12. SEM of a medial elastin laminae in the developing mouse aorta (at embryonic day 18.5) after KOH treatment. a. The elastic lamina is observed as a thin and fibrous sheet with numerous fenestrations. x 1,800. b. Closer view of the elastic lamina. The elastic lamina is composed of fine elastin fibrils, which run twodimensionally in various directions to form a thin fibrous sheet. x 11,000

“Previous TEM studies have demonstrated that bundles of microfibrils first appear during elastogenesis (ALBERT, 1972; SPICER et al., 1975). Elastin components are produced as the deposition of a small amount about 0.1 μm wide within the bundle. As the elastin components increase in number, they fuse together to become mature elastic fibers. According to our SEM studies on the extracted elastin components in the developing aorta, elastic laminae are first observed as a meshwork of fine elastin fibrils which increases in its density of elastin fibrils in the meshwork to become an elastic lamina with numerous fenestrations (Fig. 12a, b). These findings support the idea that microfibrils produce a fundamental framework of the microfibril-elastin system, which is added by the deposition of elastin fibrils about 0.1 μm thick, thus forming elastic fibers and laminae continuous with oxytalan fibers. Elaunin fibers are considered a transition form between oxytalan fibers and elastic fibers.” (Ushiki, 2002)

Conclusion by Ushiki (2002)

Fig. 13. Schematic representation of collagen fibrillar system and microfibril-clastin system. The collagen fibrillar system (green) composed of collagen fibrils which form thick bundles (i. e., collagen fibers, C) in the connective tissue and are arranged in a lace-like sheets or sheath (i. e., reticular fibers, R) attached to the basal laminae (yellow) of such cells as epithelial, endothelial or muscular ones. Thus, the collagen fibrillar system acts as a supporting framework of tissues and organs. The microfibril-elastin system is composed of microfibrils (fine solid lines) and elastin fibrils (violet), which usher in different proportions of the two components, to produce elastic (F), elaunin and oxytalan fibers (0). These three fibers of the microfibril-elastin system are continuous with one another, and form a three-dimensional network in tissues for maintaining the resilience adapted to local tissue requirements. Ep epithelium, V blood capillary, L initial lymphatic, F fibroblast.

“The present review describes the features of three major fibrous components: collagen, reticular and elastic fibers. For a comprehensive understanding of the fibrous components in connective tissues, we propose categorizing them into two systems (Fig. 13): the collagen fibrillar system and microfibril-elastin system. The collagen fibrillar system acts as a supporting framework of tissues and cells, where reticular fibers connect collagen fibers with the basal laminae of such cells as epithelial, muscle, adipose and Schwann cells. The microfibril-elastin system is composed of microfibrils and elastin fibrils, which use different proportions of the two components to produce elastic fibers, elastin fibers and oxytalan fibers. The microfibril-elastin system thus plays a role in distributing stress forces uniformly in tissues.” (Ushiki, 2002)

Eben’s Conclusion

The above discussion has several applications in the sausage-making industry. When one has raw material available such as hides/ skin, one must consider the options what the material can be used for:

  1. Skin or tendon emulsion can be made where the object is water binding;
  2. Collagen or skin chunks can be made, not to retain water but to provide firmness to the sausage matrix. In this instance it will be advisable not to hydrate the collagen or skins.
  3. If a fine emulsion is made with no show pieces, one can pre-prepare the fine skins/ tendons in the bowl chopper or micro-cutter seperately before the susage blend is made. Add the dry skin/ tendons towards the end of the blending process after all the water has been added.
  4. One must cook/ smoke with optimal crosslinking in mind.
  5. If unhydrated skin/ tendons are used, it should be possible to use a higher inclusion ratio than if its used in hydrated form.
  6. Hydration has an impact on the “solidness” of the sausage and its pastiness (resistance to bite). Amount used and hydrated or unhydrated are two of the most basic parameters which must be tested for when formulating a sausage with a high percentage of skin/ hide/ tendons included.
  7. I will incorporate the ingreadients tested by Gross (1958) and dealt with under Fibrilogenesis above, in my trails.
  8. Where resistance to boiling water is required (no gelatinization), I will be interested in, for example, the aorta which is rich in elastin fibers.

B. How are Collagen Casings made?

In this last section, I want to expose myself to more techniques used in the industry to manipulate skin or tendons. How do they do it? I first quote a traditional meat-man, explaining the basic process of producing collagen casings from beef hides.

Two Process overviews

The corium layer (splits) of USDA Approved cattle hides is extruded from between the grain (hair) layer and the fat and muscle layer. The hide consists essentially of collagen.  Protein and water are chopped and mixed with lactic acid and cellulose fibers causing them to swell and form a slurry.

The acid-swollen slurry is de-aerated under vacuum and is then homogenized and filtered to tease the collagen fibers apart.

The resultant slurry is again de-aerated and stored in chilled tanks.

It is then extruded through a die with counter-rotating sleeves, which “weave” the collagen fibers together as they pass through the die. The slurry, which is now in the form of a casing, passes directly into a concentrated coagulating solution of an inorganic salt.

The casing is then dried, partially re-humidified and wound on reels. The reels are taken to the shirring area where the collagen casing is shirred on machines similar to the type commonly used in the shirring of regenerated cellulose casings. (askthemeatman)

One of the many reasons why I think it’s counterproductive to take out a patent on certain inventions, especially chemical in nature, is because of what I am just about to do now. I refer you to US3413129A for Johnson and Johnson, invented by Emanuel R Lieberman. It is an invention of an alternative way to produce edible collagen casings. The invention was done in 1968 which makes this one of the first of its kind patents. I give the description next.


A collagen casing for sausages of the weiner or frankfurter type is manufactured by extruding a mass of acid-swollen collagen fibrils obtained from animal hide and cellulose fibers into an ammonium sulfate coagulating bath, hardening the extruded casing in an aqueous solution containing from about 0.15 percent to 10 percent by weight of ammonium hydroxide and a non-toxic ammonium salt, plasticizing the hardened casing, drying the casing. While inflated, heating the dried casing from C. to C. over a period of 8 to 12 hours, and then heating said casing for an additional 12 to 24 hours at about 80 C. This invention relates to an improved collagen casing and more particularly to extruded collagen casings that have been treated with an aqueous solution of ammonium hydroxide. While not limited thereto, the present invention is adapted to being utilized as a casing for sausages of the weiner or frankfurter type. Prior to the present invention, this type of sausage was either prepared by using expensive natural casings or inedible cellulose casing to contain the meat emulsion during the smoking and cooking process. The inedible cellulose casing must be removed by the manufacturer before the wieners are packaged for sale. The resulting product is known in the meat industry as a skinless Wiener.

There has long been a need for an extruded collagen casing that would be edible, non-toxic and sufficiently strong to stand up under stuffing, linking, smoking, washing and cooking. It is now known that edible casings for pork sausage may be prepared by extruding a tubular body from a fluid mass of swollen collagen fibrils, hardening this tubular body in the wet state and drying the collagen casing so produced. A method of producing such collagen casings is described in US. Patent No. 3,123,482.

Extruded collagen casings that are suitable for the manufacture of fresh pork sausages may not be entirely satisfactory for the production of sausages of the Wiener or frankfurter type. This is due to the differences in processing pork sausages and wieners. Thus, a meat emulsion of the pork sausage type may be stuffed, linked by twisting on a Famco linking machine, and packaged for sale without cooking. Sausages of the Wiener or frankfurter type, however, are linked on a Ty-linker, racked on a stick, smoked at temperatures from about F. to about F. or F. for several hours, rinsed with hot water at about 180 F. to F. for several minutes, and then rinsed with cold water for several minutes. The consumer may cook this product by deep fat frying, i.e., the frankfurter is plunged into a cooking oil that has been heated to 350 F. Sometimes such frankfurters have been chilled or even frozen prior to such cooking, so that the casings are subjected to great thermal stresses and pressures from steam or vapor generation. It will be appreciated, therefore, that a collagen casing used in the production of frankfurters must of necessity have a high wet strength to survive the more vigorous treatment in the linker.

An additional requirement for the frankfurter casing is that the casing should not become wrinkled and lose “ice bonding to the meat during smoking or the hot and cold rinses that follow smoking. In other words, the casing must be sufficiently elastic (not permanently deformed) so that the stress does not relax during the smoking rising cycle. On chilling after smoking, the meat contracts slightly (becomes more dense) and the casing must also shrink or the finished product will have a poor appearance.It is an object of the present invention, therefore, to produce a new and improved extruded collagen casing adapted to be utilized as a casing for sausages of the weiner or frankfurter type.

It is another object of the present invention to produce an edible casing that is exceptionally tender when eaten, yet sufficiently strong to survive linking in the Ty linker.

It is a further object of this invention to produce an edible collagen casing that will retain a smooth symmetrical appearance after smoking.

Still another object of this invention is to provide an edible collagen casing suitable for use with pork sausages or frankfurters that will not burst or peel off during cooking.

In accordance with the present invention, it has been discovered that a much improved Wiener casing may be produced by the procedure described in US. Patent No. 3,123,482 if a dilute solution of ammonia is substituted for the alum hardening agent. The use of ammonia in place of alum produces a casing that is more fragile and difficult to process during the manufacturing process. Yet the difficulty in processing is more than compensated for by the improvement in appearance and in-use performance of the finished casing.

Numerous laboratory and field tests have demonstrated that when an ammonia solution is substituted for the alum hardening solution in the process identified above, the product obtained more closely resembles natural casing. This difference is particularly apparent after stuffing, linking, smoking and cooking.

The fluid mass of swollen collagen that is extruded to form the casings of the present invention may contain from about 3.2 percent to about 4 percent by weight of collagen (calculated on the basis of dry collagen Weight) a non-collagenous filler such as cellulose or starch. If a fibrous filler such as cellulose is employed the amount may vary from about 5% to about 42% of the total solids present in the extrusion mixture. Smaller amounts of starch may be substituted for a part of or all of the cellulose.

The ammonia hardening bath may contain from about 0.15% to 10% ammonium hydroxide and from about 1% to 10% of a salt such as ammonium sulfate or ammonium lactate. To improve the wet tensile strength and elasticity of the ammonia hardened casing it is desirable to add a small amount of reducing sugar to the casing as described in US. Patent No. 3,151,990. The amount of reducing sugar employed, however, is only about one tenth of the amount required to treat an alum hardened casing. Indeed, the sugar treatment may be eliminated entirely if the ammonia hardened casing is heat-cured for a prolonged period of time, i.e., about 24 hours at 80 F.

Suitable sugars for the treatment of ammonia hardened collagen casings are reducing sugars which have a free aldehyde or keto group that is not in glucoside combination with other molecules. Examples of such reducing sugars are erythrose, threose, arabinose, ribose, xylose, cyclose, fucose, mannose, glucose (dextrose), galactose, fructose (levulose), etc. These sugars may be most conveniently applied to the collagen casing in the form of dilute solutions. The amount of sugar present in solution is related to the dwell time of the casing in the solution and the reactivity of the sugar used, and may vary from about 0.005 percent to about 0.08%. It is preferred to add the reducing sugar to the plasticizing bath, which bath follows the washing step and is the last bath contacted before the casing is dried.

Alternatively, a smoke solution derived from wood smoke vapor may replace the reducing sugar in the plasticizing bath. Smoke flavoring solutions contain a large number of acetic, phenolic and carbonyl (aldehyde) compounds that will react with collagen and improve the physical properties of the ultimate casing. The chemical constituents of smoke flavoring are discussed in’an article by Hollenbeck and Marinelli, Proceedings of the Fifteenth Research Conference, sponsored by the Research Council of the American Meat Institute Foundation of the University of Chicago, page 67 (1936). The smoke products identified in that article have been found useful in processing the ammonia hardened casings of the present invention.

The casing after it leaves the plasticizing bath is inflated and dried in a rapid stream of air and then heat cured in a forced draft oven, raising the temperature slowly from 40 C. to 80 C. during an 8 to 12 hour period. The heat treatment at 80 C. is continued for an additional 12 to 16 hours.

It will be understood that the foregoing general description and the following detailed description, as well, are exemplary and explanatory but do not restrict the invention.

The process for the manufacture of ammonia-cured collagen casings of the present invention may be more fully understood from the following detailed description and examples taken in connection with the accompanying drawings, wherein:

I include the full patent below for download.

Conclusion to Collagen Casings

The two processing overviews is enough to arm the NPD specialist with an ample starting point for investigating the production of skins/ hides and tendons to fulfil various function in fine emulsions. I refer you to the basic understanding of these emulsion type sausages in Review of comminuted and cooked meat product properties from a sol, gel and polymer viewpoint

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Ask the Meat Man

Bailey, A. J. (1978) Collagen and elastin fibres. J. clin. Path., 31, Suppl. (Roy. Coll. Path.), 12, 49-58

Gross, J., Kirks, D. (1958) The Heat Precipitation of Collagen from Neutral Salt Solutions:
Some Rate-Regulating Factors”

Kadler, K. E. (2017) Fell Muir Lecture: Collagen fibril formation in vitro and in vivo.

Jennifer Thomson, Mukti Singh, Alexander Eckersley, Stuart A. Cain, Michael J. Sherratt, Clair Baldock,
Fibrillin microfibrils and elastic fibre proteins: Functional interactions and extracellular regulation of growth factors, Seminars in Cell & Developmental Biology, Volume 89, 2019, Pages 109-117, ISSN 1084-9521, (

Ushiki, T.. (2002) Collagen Fibers, Reticular Fibers and Elastic Fibers. A Comprehensive Understanding from a Morphological Viewpoint. Division of Microscopic Anatomy and Bio-imaging, Department of Cellular Function, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan

Nitrite Cured Meat: It’s Fantastic but is it also Bad?

Nitrite Cured Meat: It’s Fantastic but is it also Bad?
By Eben van Tonder
15 February 2021


I started my career in meat curing in 2008 when I founded the South African bacon brand Woody’s and the company Woody’s Consumer Brands with Oscar and Anton. I never imagined that the most exciting journey on earth would follow which I chronicled in Bacon & the Art of Living. I wanted to know as much as possible about the world of curing and the chemical, biological and bacterial reactions that fascinated me. One of the first books I consumed was Ronald Pegg and Fereidoon Shahidi’s work, Nitrite Curing of Meat: The N-Nitrosamine Problem and Nitrite Alternatives.

I delved into the matter with great interest. I discovered that nitrates are present in many vegetables, but they first need to change to nitrites through bacterial action before they change chemically into nitric oxide which then cures the meat. Nitrates are not very toxic, but once they change into nitrite and is fried, their reaction in the stomach is of particular concern.

As I learned more I discovered the importance of cured products in a world before refrigeration. They are extremely effective to protect us against pathogens, including the mother of all pathogens, Clostridium Botulinum. Its protective action extends into the age of refrigeration! Far from a villain chemical, it turns out that nitrite is an amazing compound that naturally occurs all around us and is, amongst others, formed in our mouths when we consume a wide variety of food including fruits and vegetables.

The question is now obvious. We know that adding nitrites to meat is doing a world of good in giving us safe food that lasts long without refrigeration and just happens to also taste delicious but are we causing more harm than good? Should we stop using it if we ingest far more nitrites from some vegetables than from cured meat? How do we evaluate a matter when scientists continually conclude any discussion on the matter with the words “more research on the topic is required?”

When did we realise that nitrite is not only beneficial but under certain conditions may be problematic? What exactly is the concern with its use? How did we end up using this? What physiological role does it play in humans? What benefits do we derive from ingesting it?

I will provide a brief overview. More than this, I use this as a landing page for material on the subject. Some of my consultancy work relates to exactly this topic and proprietary information is therefore restricted with password protection. Why “password” protected? Because the obvious next question is this: “Is there anything we can do to change it?” To manage the negative elements so that it is removed, and the product is wholly healthy! The answer is a resounding YES! But that is proprietary information! 🙂

A. How did we Realise there is a Problem?

What is the actual issue then and how did humans realise that there is a problem?

The Realization of Danger of Nitrites in Cured Meat and The Responses Since 1926

Nitrate was used as a curing agent for many thousands of years. The basic value initially related to the preventing of spoilage and in a world before refrigeration bacon soon became the staple meat source for the masses in a large part of the world. Curing with saltpetre, the common name for nitrate salts, takes about a month and apart from retarding spoilage, it imparts into meat a characteristic pinkish/ reddish colour and a very agreeable cured meat taste. In the 1800s a new method of curing was invented which reduced the time to cure meat considerably. It was called tank curing on account of the tanks that were used to cure the meat in or mild curing due to a reduced need for salt. It was invented in Ireland. When our understanding of chemistry and bacteriology matured, we realised the reason why tank curing sped meat curing up. For curing to take place nitrate (saltpetre) must first be converted to nitrite through bacterial action before it can be changed into nitric oxide which, we discovered, is the real curing molecule. So, nitrate (saltpetre) to nitrite curtesy of microorganisms (bacteria) and nitrite to nitric oxide through is a chemical reaction.

What was achieved through tank curing was that the step of bacteria changing nitrate into nitrite is cut out. Still, we do not add the nitrite directly. It is “added” through fermentation. The old brine is re-used and in doing so, the liquid is replete with nitrite that was already converted from nitrate. This, naturally, speeds the process up by cutting a step out. Before the late 1800’s curers did not have a clue what caused curing apart from saltpetre. They arrived at the process of tank curing through experimentation and observation without any inkling to microorganisms changing nitrate to nitrite.

The curing reaction was being unravelled by scientists late in the 1800s and early in the 1900s. As we learned that going from nitrite to nitric oxide is much quicker than going from nitrate first to nitrite and then to nitric oxide. We also realized that nitrite forms a salt with sodium to create sodium nitrite. Late in the 1800s and early in the 1900s sodium nitrite was being used in the dye industry and chemists stocked it because it became an important medication to treat some blood disorders. Butchers used it as the source of nitrite. It is easier and “cleaner” than the indirect creation of nitrite through fermentation (tank curing or mild curing). Sodium nitrite can be dissolved directly in a brine and will immediately start penetrating the meat and change to nitric oxide.

Tank curing soon lost its place as the quickest way to cure meat in favour of the direct addition of nitrites to curing brines. There was an issue with nitrites though in that most people at this time knew that nitrite was a potent toxin. Understandably, from very early, humans who did not “see” the conversion of nitrate to nitrites and did not understand that nitrites were in any event present in cured meat grappled with the concept of a toxic substance being introduced in food preparations.

During the First World War, curing brines came onto the market which included nitrites. The days of tank curing were numbered, and a controversy was born about how healthy this is. Several investigations were made into the matter. No sooner was the matter of the toxicity of nitrites settled through scientific investigation when another, far more dangerous issue came onto the scene in the 1970s of n-nitrosamines. Let’s run through the chronology of some of the key studies and some of the important ways that governments around the world responded to it.

We picked the investigations into this matter up in 1926 which looked at the matter of nitrite as a toxin. If it was simply a matter of concentration, it would be easily settled because we regularly use substances if food which, in too high dosages can harm or even kill us. Alcohol is a very good example. The way to mitigate the risk is to determine the “safe” levels and to ensure that producers use the appropriate dosages.


A 1926 study by Kerr and co-workers was based on the general knowledge of nitrite’s toxicity and the publics very negative perceptions about it.  In the report, they state that public health was the primary motivation behind the study.  (Kerr, et al, 1926: 543)  I quote from their report.  “The first experiment involving the direct use of nitrite was formally authorized January 19, 1923, as a result of an application by one of the large establishments operating under Federal meat inspection. Before that time other requests for permission to experiment with nitrite had been received but had not been granted. The authorization for the first experiment specified that the whole process was to be conducted under the supervision of bureau inspectors and that after the curing had been completed the meat was to be held subject to laboratory examination and final judgment and would be destroyed if found to contain an excessive quantity of nitrites or if in any way it was unwholesome or unfit for food. This principle was rigidly adhered to throughout the experimental period, no meat being passed for food until its freedom from excessive nitrites had been assured, either by laboratory examination or through definite knowledge from previous examinations, that the amount of nitrite used in the process would not lead to the presence of an excessive quantity of nitrites in the meat. By “excessive” is meant a quantity of nitrite materially in excess of that which may be expected to be present in similar meats cured by the usual process.”  (Kerr, et al, 1926: 543)

The maximum nitrite content of any part of any nitrite-cured ham [was found to be] 200 parts per million. The hams cured with nitrate in the parallel experiment showed a maximum nitrite content of 45 parts per million.”  (Kerr, et al, 1926: 543) The conclusion was that “hams and bacon could be successfully cured with sodium nitrite, and that nitrite curing need not involve the presence of as large quantities of nitrite in the product as sometimes are found in nitrate- cured meats.”  (Kerr, et al, 1926: 545)

Related to the health concerns, the report concluded the following:

  1. The presence of nitrites in cured meats, was already sanctioned by the authoritative interpretation of the meat inspection and pure food and drugs acts sanctioning the use of saltpeter; as shown previously, meats cured with saltpeter and sodium nitrate regularly contain nitrites. (Wiley, H, et al, 1907) (Kerr, et al, 1926 : 550)
  2. The residual nitrites found in the nitrite-cured meats were less than are commonly present in nitrate-cured meats.  The maximum quantity of nitrite found in nitrite-cured meats, in particular, was much smaller than the maximum resulting from the use of nitrate.  (Kerr, et al, 1926 : 550)
  3. The nitrite-cured meats were also free from the residual nitrate which is commonly present in nitrate-cured meats.  (Kerr, et al, 1926 : 550)
  4. On the contrary, the more accurate control of the amount of “nitrite and the elimination of the residual or unconverted nitrate are definite advantages attained by the substitution.  (Kerr, et al, 1926 : 550)

Following further studies, the Bureau set the legal limit for nitrites in finished products at 200 parts per million.  (Bryan, N. S. et al, 2017: 86 – 90) Conventional wisdom that surfaced in the 1920s suggested that nitrate and nitrate should continue to be used in combination in curing brines (Davidson, M. P. et al; 2005:  171) as was the case with the Irish curing method or the tank curing concept of the previous century. Nitrite gives the immediate quick cure and nitrate acts as a reservoir for future nitrite and therefore prolongs the supply of nitrite and ensures a longer curing action.  This concept remained with the curing industry until the matter of N-nitrosamines came up in the 1960s and ’70s, but remarkably enough, it persists in places like South Africa where to this day, using the two in combination is allowed for bacon. More about this later.


The USDA progressed the ruling on nitrate and nitrites further in 1931 by stating that where both nitrites and nitrates are used, the limit for nitrite is 156 ppm nitrite and 1716 nitrate per 100lb of pumped, cured meat.  (Bryan, N. S. et al, 2017: 86 – 90)

1960’s – N-Nitrosamine

Up to the 1960’s the limit on the ingoing level of nitrites was based on its toxicity.  In the late 1950s an incident occurred in Norway involving fish meal that would become a health scare rivalled by few in the past.  1960’s researchers noticed that domestic animals fed on a fodder containing fish meal prepared from nitrite preserved herring were dying from liver failure. Researchers identified a group of compounds called nitrosamines which formed by a chemical reaction between the naturally occurring amines in the fish and sodium nitrite.  Nitrosamines are potent cancer-causing agents and their potential presence in human foods became an immediate worry.  An examination of a wide variety of foods treated with nitrites revealed that nitrosamines could indeed form under certain conditions.  Fried bacon, especially when “done to a crisp,” consistently showed the presence of these compounds. (Schwarcz, J) In bacon, the issue is not nitrates, but the nitrites which form N-nitrosamines.

This fundamentally sharpened the focus of the work of Kerr and co-workers of the 1920s in response to the general toxicity of nitrites to the specific issue of N-nitrosamine formation. Reviews from 1986 and 1991 reported that “90% of the more than 300 N-nitroso compounds that have been tested in animal species including higher primates causes cancer, but no known case of human cancer has ever been shown to result from exposure to N-nitroso compounds.”  However, despite this, there is an overwhelming body of indirect evidence that shows that a link exists and “the presence of N-nitroso compounds in food is regarded as an etiological risk factor.   It has been suggested that 35% of all cancers in humans are dietary related and this fact should not surprise us.  (Pegg and Shahidi, 2000)

Studies have been done showing that children who eat more than 12 nitrite-cured hot dogs per month have an increased risk of developing childhood leukaemia.  The scientists responsible for the findings themselves cautioned that their findings are preliminary and that much more studies must be done.  It may nevertheless be a good approach for parents to reduce their own intake of such products along with that of their children in cases where intake is high.  (Pegg and Shahidi, 2000)

These studies must be balanced by the fact that an overwhelming amount of data has been emerging since the 1980s that indicate that N-nitroso compounds are formed in the human body.  What is important is that we keep on doing further research on N-nitrosamines and the possible link to cancer in humans.  Not enough evidence exists to draw final conclusions.

1970 – The response to the N-Nitrosamine scare.

Back in the 1970s, so grave was the concern of the US Government about the issue that in the early 1970’s they seriously considered a total ban on the use of nitrites in foods. (Pegg and Sahidi, 2000) The response to the N-nitrosamine issue was to go back to the approach that was implemented following the work of Kerr and co-workers in 1926.

The first response was to eliminate nitrate from almost all curing applications.  The reason for this is to ensure greater control over the curing. Meat processors continued to use nitrate in their curing brines from 1920 until the 1970s. One survey from 1930 reported that 54% of curers in the US still used nitrate in their curing operations.  17% used sodium nitrite and 30% used a combination of nitrate and nitrite.  By 1970, 50% of meat processors still used nitrate in canned, shelf stable.  In 1974 all processors surveyed discontinued the use of nitrates in these products including in bacon, hams, canned sterile meats, and frankfurters.  One of the reasons given for this change is the concern that nitrate is a precursor for N-nitrosamine formation during processing and after consumption.  (Bryan, N. S. et al, 2017: 86 – 90)

The reason for the omission in bacon, in particular, is exactly the fact that the nitrates will, over time continue to be converted to nitrites which will result in continued higher levels of residual nitrites in the bacon compared to if only nitrite is used.  The N-nitrosamine formation from nitrites is a reaction that can happen in the bacon during frying or in the stomach after it has been ingested.  It will not happen from the more stable nitrates.

It has been discovered that nitrate continues to be present in cured meats.  Just as the view that if nitrate was added, no nitrite is present in the brine as was the thinking in the time before the early and mid-1800s, in exactly the same way it is wrong to think that by adding nitrite only to meat, that no nitrate is present.  “Moller (1971) found that approximately 20% of the nitrite added to a beef product was converted to nitrate within 2 hours of processing.  Nitrate formation was noted during incubation before thermal processing, whereas after cooking only slight nitrate formation was detected.  Upon storage, the conversion of nitrite to nitrate continued.  Herring (1973) found a conspicuous level of nitrate in bacon formulated only from nitrite.  As greater concentrations of nitrite were added to the belly, a higher content of nitrate was detected in the finished product.  They reported that 30% of the nitrite added to bacon was converted to nitrate in less than one week and the level of nitrate continued to increase to approximately 40% of the added nitrite until about 10 weeks of storage.  Moller (1974) suggested that when nitrite is added to meat, simultaneous oxidation of nitrite to nitrate and the ferrous ion of CodeCogsEqn (5)  to the ferric ion of metMb occurs.” Adding ascorbate or erythorbate plays a key role in this conversion.  (Pegg and Shahidi, 2000)  The issue is not the nitrate itself, but the uncontrolled curing that results from nitrate and the higher residual nitrites.

Secondly, the levels of ingoing nitrite were reduced, especially for bacon.  The efficacy of these measures stems from the fact that the rate of N-nitrosamine formation depends on the square of the concentration of residual nitrites in meats and by reducing the ingoing nitrite, the residual nitrite is automatically reduced and therefore the amount of N-nitrosamines.  (Pegg and Sahidi, 2000) Legal limits were updated in 1970 in response to the nitrosamine paranoia. A problem with this approach is however that no matter by how much the ingoing nitrite is reduced, the precursors of N-Nitrosamine still remain in the meat being nitrites, amines, and amino acids.

An N-nitrosamine blocking agent was introduced in the form of sodium ascorbate or erythorbate. “There are several scavengers of nitrite which aid in suppressing N-nitrosation; ascorbic acid, sodium ascorbate, and erythorbate have been the preferred compound to date.  Ascorbic acid inhibits N-Nitrosamine formation by reducing CodeCogsEqn (11)  to give dehydroascorbic acid and NO.  Because ascorbic acid competes with amines for CodeCogsEqn (11), N-Nitrosamine formation is reduced.  Ascorbate reacts with nitrite 240 times more rapidly than ascorbic acid and is, therefore, the preferred candidate of the two.  (Pegg and Sahidi, 2000)

More detailed studies identified the following factors to influence the level of N-nitrosamine formation in cured meats.  Residual and ingoing nitrite levels, preprocessing procedure and conditions, smoking, method of cooking, temperature and time, lean-to-adipose tissue ratio, and the presence of catalyst and/ or inhibitors.  It must be noted that in general, levels of N-nitrosamines formation have been minuscule small, in the billions of parts per million, and sporadic.  The one recurring problem item remained fried bacon.  In its raw state bacon is generally free from N-nitrosamines “but after high-heat frying, N-nitrosamines are found almost invariably.”  One report found that “all fried bacon samples and cooked-out bacon fats analyzed” were positive for N-nitrosamines although at reduced levels from earlier studies.  (Pegg and Sahidi, 2000)

Regulatory efforts since 1920 have shown a marked decrease in the level of N-nitrosamines in cured meats, even though it is still not possible to eliminate it completely.  “Cassens (1995) reported a marked decrease (approx 80%) in residual nitrite levels in of US prepared cured meat products from those determined 20 years earlier; levels in current retail products were 7 mg/kg from bacon.”  This and similar results have been attributed to lower nitrite addition levels and the increased use of ascorbate or erythorbate.  (Pegg and Sahidi, 2000)

Despite the actions of governments and the curing industry, consumer demand has grown over the years to eliminate nitrites in food. Evidence has started to emerge that links the prevalence of colon cancer, for example, not just to the use of nitrites but to the use of saltpetre or the far less toxic cousin of nitrite called nitrate. Much of the evidence is either anecdotal or indirect but it is sufficient to fuel public suspicion and legitimate industry concerns.

B. Can’t we just Remove the Nitrites?

What is clear from our survey above is that it is a technical and complex field. Can we not just remove the nitrites and sell nitrite-free bacon? When we talk about nitrite-free bacon, it is important to know exactly what we are talking about. The term can imply several things.

– Is the Problem Synthetic Nitrites Only (I.e. Sodium Nitrite Added Into the Brine)?

Is it that no synthesized nitrite must be used in the curing of the meat? Tank curing or fermented nitrate containing plant juices would then be an appropriate curing procedure. Celery and other plants are filled with nitrates which are part of plant nutrition, absorbed from the soil through the roots. Certain spice companies started using these plant extracts and then through a process of fermentation, allowed microorganisms to reduce the nitrite to nitrate like what was done in tank curing using old brine and they sold the plant extracts to be added to the meat as an ingredient. They called it a “natural curing agent” but in my opinion, they were actually deceiving the public. After the bacterial fermentation, the plant juices were now filled with nitrates. They cleverly circumvented the requirement to declare the use of nitrites in the curing process and in reality, nitrites were still present, now in usually much larger quantities as was the case using sodium nitrite.

– Is the Problem All Nitrites in the Brine and Meat, Including Either Sodium Nitrite or Nitrite that Formed Through Bacterial Action, Either through Reduction or Oxidation or Chemically and Irrespective of the Source?

Nitrite-free bacon can mean that no nitrites should be used in the curing process added directly or generated indirectly. Indirectly it can be generated through fermentation but there are other sources of nitrite which forms as a result of the decomposition of meat. In long-term curing, for example, the same colour, even a better taste and longer shelf life is achieved by the use of salt only. I mention this because it introduces a very important issue. For curing to take place, you don’t actually need nitrate or nitrite. You need nitrogen. The nitrogen must then react with oxygen to create nitric oxide (NO) which is a gas! Nitrate and nitrite are only the nitrogen source! Once Nitric Oxide is created, it must react with the meat proteins, myoglobin.

As the proteins of a dead animal or other constituents of meat are being broken down, nitrogen is made available and in long term curing, certain processes are involved and one of them is the combination of the nitrogen molecule, made available through decomposition, with an oxygen molecule and curing takes place if the overall destruction of the meat is managed through the removal of water which retards (even stops) the action of microorganisms and favours the effect of enzymes.

So, this can be done completely without any outside source of nitrogen but the process is very slow and there is no way that the world demand for cured meat will be satisfied through this. It will also be extremely expensive due to the weight loss involved in removing the moisture. No matter how you look at it, nitrogen must be accessed somehow, or it is not curing.

It is extremely important to know that curing is something that happens to the meat itself and it mimics a natural, biological process of nitric oxide being formed in our bodies. The meat protein in either its oxygenated state or with a nitric oxide molecule presents red. This is an extremely important concept to understand. Curing is a characteristic of meat itself and is a natural process. It is NOT the imposition upon the meat of a colouring agent. The fact that nitrogen is used in curing is completely consistent with natural biological processes. Even the reduction and interaction of nitrate and nitrite, including the chemical reduction to nitric oxide, is a biological process, essential to life!

I give one example from a review article by Shiva (2013). I anticipate that very soon consumers may demand food with high nitrate (NO3-) in a swing in perceptions of these molecules which will in all likelihood be driven by people who regularly work out. Shiva summarizes this work as follows. “Nitrite dependent inhibition of ccox also potentially regulates responses to physiological hypoxia (the absence of enough oxygen in the muscles), such as that present in the muscle during exercise. Larsen and colleagues recently demonstrated that ingestion of NO3- (nitrate) decreased whole-body oxygen consumption during exercise without changing maximal attainable work rate in human subjects.” Directly as a result of this work, several booster supplements are currently on the market and sold in gyms and health shops around the world containing nitrates.

Shiva continues, “This increase in exercise efficiency, which was associated with augmented plasma NO2- levels, has now been corroborated by a number of studies in various exercise models. While the underlying mechanism of this beneficial effect is not completely elucidated, a decrease in the rate of oxygen consumption due to proton leak and state 4 respiration in the skeletal muscle of subjects receiving NO3- was reported.” (Shiva, 2013)

Right there, the entire matter is resolved and in a few short years, the public will demand more nitrates in meat (and by implication, nitrite also)! 🙂 🙂

Furthermore, not only is the reaction of nitrite to nitric oxide not foreign in our physiology, the reaction of nitric oxide with myoglobin is an extremely important physiological reaction that is mimicked in curing. Jens Moller and Leif Skibsted write that “Nitrosylmyoglobin (MbFeIINO), the NO complex of iron (II) myoglobin, as formed in meat products, has now also been observed in vivo in rats. MbFeIINO thus seems important in controlling radical processes associated with oxidation”. (Møller and Skibsted, 2002)

The issue is that our best available source of nitrogen is through nitrite and nitrite itself but is both beneficial and problematic at the same time.

The fact that the reaction of oxygen (O2) and Nitric Oxide are both matters that all butchers work with daily is important. None of these reactions is “unnatural!” This is seen in the colour of fresh meat and cured meat. I dedicated a chapter to it in Bacon & the Art of Living, called Fresh Meat Colour vs Cooked Cured Colour.

I plan to do much more work about the physiological reason why nitric oxide fits onto the colouring site of a protein apart from the short quotes above, but I will deal with this separately and update this section with a link reference.

– If the Meat itself Does Not Change Colour (Curing), is the use of External Colourant Permitted/ Desirable?

There is another way of achieving a red colour in meat which we alluded to and that is through an artificial process that involves the use of an external colourant. Legally there are colourants that are allowed in meat, but how will consumer groups respond to this? This is not something natural and inherently part of meat itself. It is an external colourant that is brought to bear upon the meat matrix. This is even more objectionable to some than nitrite and the extreme objection against it goes back to the start of the meat trade where butchers used to disguise old and sometimes putrid meat as fresh by colouring it with an external colourant.

– Is the Real Issue Actually Residual Nitrite That We Must Eliminate? (I.e., Not Ingoing Nitrite but Nitrite Left in Meat After Curing)

Another possible meaning of nitrite-free bacon refers not to the fact that nitrite was somewhere involved in the supply of the nitrogen source to form nitric oxide, but the real meaning may refer to the question of whether any nitrite is left in the product when the consumer fries it in the pan. It is after all not the initial source of the nitrogen atom, which is the real issue, but how much nitrite is left after the meat has been cured. This is what is referred to as residue nitrite. The other question which goes hand in hand with this is to what degree can the consumer be guaranteed that no appreciable amount of nitrite is left in the product he buys?

– Is The Objective to Eliminate All Manipulation of Colour (Natural or Artificial) and Resign Ourselves to Selling Brown Bacon and Hams (uncured, salted only)?

A final solution for some is to simply omit accessing nitrogen in any shape or form altogether and not be concerned about the brownish colour that develops. I have over a few years followed the work of a New Zealand company, interestingly enough also called Woody’s who follow this approach and I am amazed at the success they have had with their brand positioning. Good old strict hygiene is used to sort shelf-life issues out and they educate their customers that the browner bacon is actually healthier bacon. The brown bacon they sell becomes a source of comfort for their clients. If this is advisable as a universal approach to bacon or ham is debatable in a world where not everybody shares the strict attention to detail of this company, but I applaud them for their honesty and the practical way in which they have dealt with this thorny issue (see Woody’s Free Range Farm) In the end, I feel much of the problems are self-inflicted in a world where bacon flitches are no longer wrapped in cloth, palletized and shipped any longer.

By William James Topley – This image is available from Library and Archives Canada under the reproduction reference number PA-026092 and under the MIKAN ID number 3424485

How to Explain it?

As you can see from this short overview, the matter is not simple but the fact that there is an issue to address is clear. For myself, I am satisfied that in the minuscule levels that nitrite is used and remains present in bacon and hams, these products are completely safe to eat. The consumer is, however, also not wrong to be concerned about the matter. The problem is that the explanation above is already so technical – who can follow this? Let alone a dissertation by Dr Sebranek or Dr Møller, two of the world authorities on the subject. If anybody must understand what they are saying before one can decide which bacon is healthy and not and which brine to use or not, only a handful of people will ever make a meaningful determination on the matter. This business of reduction and oxidation, bacterial, enzymatic reactions are all very confusing for people without an advanced degree in chemistry, like me. The only way that I could make any sense of it was to follow the story right from the beginning. As it unfolded. And what a story it turned out to be!

C. Review: How did we get here?

I will tell the story, at least the parts that are pertinent to the discussion about nitrite, from a series of articles I did on the subject over a few years and from extracts of a book I wrote about the history of bacon called Bacon & the Art of Living. One article where I deal with the full sweep of its history is Bacon Curing – a Historical Review.

Before we jump into the detail, let’s establish a timeline. Broadly speaking the development of bacon curing to where we are with the direct addition of nitrite to curing brine can be divided into the following timeline.

  • The Prehistory of Bacon Curing experimenting with various salts (sodium chloride, sal ammoniac, nitrate also called saltpetre) From antiquity to the end of the 1500s.

  • Saltpetre gained popularity as it becomes widely available as a vitalizer, an ingredient in gunpowder and as medication. 1600 to 1800.

  • William Oake invented Tank Curing/ Mild Curing around 1832 (aged 25) – an Indirect Addition of Nitrite to Curing Brines.

  • Dr. Ed Polenski’s Article on Nitrite in saltpetre brines, 1891.

  • The academic work of German and English researchers identifying Nitrate and Nitric Oxide as the curing agents. Notwang (1892), Lehmann (1899), Kiskalt (1899), Haldane (1901).

  • The work of Ladislav Nachmullner and the first curing brine containing sodium nitrite (1915).

  • The Impact of the First and Second World War in changing the indirect use of Nitrites to the direct addition of nitrites to curing brines.

  • The Griffith Laboratories as evangelists of the direct addition of nitrites to curing brines. Prague Salt (1925).

  • “Houston, we have a problem!” The n-nitrosamine problem and the response of the curing industry and world governments, late 1950s.

  • Must we Remove Nitrite from Food or Manage it?

D. Why do we use it at all?

Its anti-microbial ability now becomes important, especially as it relates to C Botulinum. Nitrite as a key hurdle in botulinum prevention remains relevant. I looked at the most important microorganism in a 2015 article, Clostridium Botulinum – the priority organism

The Anti-Microbial Efficacy of Nitrite

In 2015 I had the privilege to interact with Dr R. Bruce Tompkin on the issue of the antimicrobial efficacy of nitrate and nitrite. Dr Tompkin was one of the founders of the HACCP system. We had some correspondence about the possibility of replacing nitrite as a hurdle and his insights are still helpful to this day. For this, I will be eternally grateful. It was written before I discovered that tank curing came from Ireland and there are other sections where my understanding evolved. I nevertheless share it with you as I wrote five years ago. I am thankful for experts from around the world who continue taking the time to give input not just on the matter of nitrite replaces, but on a wide array of meat and processing-related subjects. I can honestly say that if you do not know in our trade you do not want to know! (or you have been so busy that there was no time to find out!) 🙈🙈 Which I fully understand!! 🤣🤣

I looked at this issue in 2015 in an article, Concerning Nitrate and Nitrite’s antimicrobial efficacy – chronology of scientific inquiry.

E. Further Work on Nitrite Free Bacon and its role in Human Physiology


I have no doubt that this matter can be resolved scientifically. In terms of marketing, this can be done in a way that the consumer will be fully in-step, all the way and is taken along, not left behind or feel that half-baked ideas are thrust down his/her throat. This work is important, not just for the uncompromising drive to better and healthier food, but for the overall quest to be better in every way! To offer safe and delicious food should be the desire of every food producer on earth. Anything less both in terms of taste, quality, and safety is a crime! In this work, I can end with a quote from no finer man than Nelson Mandela who said that “what counts in life is not the mere fact that we lived. It is what difference we have made to the lives of others that will determine the significance of the life we lead!”


Jens K. S. Møller and Leif H. Skibsted. 2002. Nitric Oxide and Myoglobins. Chemical Reviews 2002102 (4), 1167-1178DOI: 10.1021/cr000078y

Beef Heart Pastrami

Milen Nenchev (Милен Ненчев) from Sofia, Bulgaria shared details of Beef Heart Pastrami he made. The work is of such quality that I had to include it in my list of artisan recipes.

He writes, “Harvest wasn’t going well so I thought I’d make the cats a Christmas present but decided to taste it before making the final decision…!? A gross mistake I would have made if I hadn’t tried. Unfortunately, the kittens will be left without a gift!!! 😁

Controlled salting for 10-12 days.
The right amount of spices for 1000 grams
30 grams of salt (12 nitrite / 18 plain)
5 grams of sugar
5 grams of black pepper
5 grams of conifer
2 grams of cumin
2 grams of pride
3-4 pcs of cloves
1 gram of cardamom
50 ml of red wine
Cheers! 🍷

There are other Beef Heart Pastrami recipes on the web, but this is my favourite due to the low water activity and the possibility to create another biltong hybrid! I include this on my list of artisan products to make. Shall I call it Milen (Милен)-Biltong? I like the name! 🙂


Ladies and gentlemen, licantropes! ☠☠☠ Good news for horror lovers and fans of brutal music. In my attempts to create something different, more interesting, better… I present to your attention the experiment that exceeded all expectations. Here is the final continuation of the saga “Lukanka from a Beef Heart”❤❤❤

Milen Nenchev (Милен Ненчев) not only made beef heart pastrami but also sausages.

One of his friends, Nikolay Nikolov (Николай Николов) made an interesting comment worth noting. He wrote, “I have done a lot of experiments, beef heart and pork 50/50, 60/40 and one sample of beef heart only, a perfect sausage is always obtained, I also put pork hearts instead of beef and it still works, the woman likes more the one with hearts than the one with only meat.”

Very special people live around the Black Sea with a natural “feeling” for meat that goes back thousands of years! It shows!

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Westphalian Hams and Bacon Recipes


Westphalia is a region in Germany from where the most iconic hams in the history of ham making came. A key feature of the ham is that it is cold smoked. I give the complete list of Westphalian ham and bacon recipes available to me below. I suggest you read through all of them carefully and develop your own particular recipe. The two key features of the ham and bacon are that it must be cold smoked and I would use the Emperor of Russia’s Brine recipe, but it all depends on your own preference.

Background to Westphalian Ham

For the sake of authenticity, I suggest before attempting Westphalian ham or bacon, you read as background the following article: Westphalia Bacon and Ham & the Empress of Russia’s Brine: Pre-cursers to Mild Cured Bacon. The importance of cold smoking will become clear as well as using the right brining approach.

A Westphalian Ham and Bacon Recipes

-> From the Unknown American Cookbook

A very old American recipe book gives the recipe for Westphalian Ham as follows.  The process is dry curing.

Pork – 100
Salt – 4
Water or Ice – 20
Na or K Nitrate – 1

Hams Rubbed with salt and saltpeter.
Place in vat.
Cure, 4 weeks.
Air dry, 4 days.
Smoke with dry wood and juniper.

-> From the New Cyclopedia of Domestic Economy and Practical Housekeeping

The 1872 publication edited by Ellet, E. F and published by H. Bill, Norwich, Conn. boast “five thousand practical receipts and maxims from the best English, French, German, and American sources.” I quote the following from his work, The New Cyclopedia of Domestic Economy and Practical Housekeeping


As soon as the pig is cold enough to be cut up, take the two hams, and cut out the round bone, so as to have the ham not too thick: rub them with common salt, and leave them in a large pan for three days; when the salt has drawn out all the blood, throw the brine away, and proceed as follows: for two hams of about eighteen pounds each, take one pound of moist sugar, one pound of common salt, and two ounces of saltpetre, mix them together, and rub the hams well with it, then put them into a vessel large enough to contain them in the liquor, always keeping the salt over them; after they have been in this state three days, throw over them a bottle of good vinegar. One month is requisite to cure them; during which period they must be often turned in the brine; when you take them out, drain them well, powder them with some coarse flour, and hang them in a dry place. The same brine will serve again, except that you must not put so much salt on the next hams that you pickle. If the hams are smaller, put only three-quarters of a pound of salt, but the salt will not do any harm if you do not let them remain too long in the brine; if you can get them smoked, they are then not so subject to be infested by vermin; no insect whatever can bear the bitterness of the soot; the smoke of wood is preferable to the smoke of coal. Be particular that the hams are hung as far as possible from the fire, otherwise the fat will melt, and they will become dry and hard and rank.

The following are recipes collected from around the world by


Prepare the hams in the usual manner by rubbing them with common salt and draining them; take one ounce of saltpetre, half a pound of coarse sugar, and the same quantity of salt; rub it well into the ham, and in three days pour a pint of vinegar over it. A fine foreign flavor may also be given to hams by pouring old strong beer over them, and burning juniper wood while they are drying: molasses, juniper berries, and highly flavored herbs, such as basil, sage, bay leaves, and thyme, mingled together and the hams well rubbed with it, using only a sufficient quantity of salt to assist in the cure, will afford an agreeable variety.


Sprinkle each flitch with salt; and let the blood drain off for twenty – four hours. Then mix one pound and a half of coarse sugar, the same quantity of fine salt, six ounces of saltpetre, and four pounds of coarse salt; rub this well on the bacon, turning and wetting it in every part daily for a month; then hang it to dry, and afterwards smoke it ten days.

925. – A PICKLE

That will keep for years, for hams, tongues, or beef, if boiled and skimmed between each parcel of them. To two gallons of spring water put two pounds of coarse sugar, two pounds of coarse, and two and a half pounds of common salt, and half a pound of saltpetre, in a deep earthen glazed pan that will hold four gallons, and with a cover that will fit close. Keep the beef or hams as long as they will bear before you put them into the pickle; and sprinkle them with coarse sugar in a pan, from which they must drain. Rub the hams, & c., well with the pickle; and pack them in close, putting as much as the pan will hold, so that the pickle may cover them. The pickle is not to be boiled at first. A small ham may lie fourteen days; a large one three weeks; a tongue twelve days; and beef in proportion to its size. They will eat well out of the pickle without drying. When they are to be dried, let each piece be drained over the pan; and when it will drop no longer, take a clean sponge and dry it thoroughly. Six or eight hours will smoke them; and there should be only a little sawdust and wet straw burnt to do this; but if put into a baker’s chimney, sew them in a coarse cloth, and hang them a week. Add two pounds of common salt, and two pints of water, every time you boil the liquor.

Have a Westphalian recipe?

If you have a Westphalian recipe, please share it with me for inclusion here. or whatsapp on +27 071 5453029.

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Westphalia Bacon and Ham & the Empress of Russia’s Brine: Pre-cursers to Mild Cured Bacon

Westphalia Bacon and Ham & the Empress of Russia's Brine: Pre-cursers to Mild Cured Bacon 
Eben van Tonder
18 December 2021

-: Dedicated to my Son, Tristan van Tonder who is 24 today and Shanonnon Hounsell who share his life and his birthday! You have been part of so many quests and discoveries! What an amazing world we live in! :-


The study of Westphalia Bacon and Ham smoking techniques and the Empress of Russia’s Brine leads us to one of the most astonishing discoveries about the history of curing since I uncovered the role of the First World War and the direct addition of nitrites to curing brines. (The Direct Addition of Nitrites to Curing Brines – the Master Butcher from Prague and The Direct Addition of Nitrites to Curing Brines – The Spoils of War) Whether fermentation or through adding nitrites directly, curing is dependent upon nitric oxide formation from nitrite salts. How nitrite salts are accessed brought about two roads that run parallel and have been for hundreds of years. The direct and most recent development in curing where nitrite salts are used instead of nitrates. The first curing salt where this was included was Praganda from the city of Prague. Griffiths Laboratories brought out Prague Salt and soon afterwards Prague Powder and became the international evangelists of this new curing system. Before this, nitrite salts were accessed through deliberate fermentation in the system that was invented by William Oake in Northern Ireland (Mild Cured Bacon), was exported to Denmark through disgruntled striking bacon workers (The Danish Cooperative and Saltpeter) and became Wiltshire cure or tank curing or the live brine system which was so typical of English bacon (Wiltshire Cured or Tank Cured Bacon). The power of the old brine is in the fact that nitrate salts have been reduced to nitrite salts through bacterial fermentation. By re-using the old brine, one now has a brine with nitrites in it already and curing speed is vastly improved. I never dreamt that I would be able to discover how this was brought about? Why did people start to re-use the old brine? What forces caused people to start using it? A study of Westphalian bacon and ham and the Empress of Russia’s Brine leads me to the discovery of the origins of what later was progressed and composed into a complete system by the Northern Ireland chemist, William Oake. (Mild Cured Bacon) Unravelling the mechanism of moving from an immersion brine with dry salting to start re-using the brine was completely unexpected and, in the end, became one of the most thrilling discoveries of my career!

The Primitive Descriptions of Dr Cogan

It started with a study of Westphalian ham and bacon. A description of the process is given by Dr Cogan who toured the region of Westphalia. His description comes to us from a 1796 newspaper article. His language could be a bit clearer, and considering it carefully, he seems to be speaking about the application of stove technology in the houses in Westphalia in the 1700s.

He describes the Scheuren or Barns where the people lived as housing a small family and their livestock. Hogs and poultry occupied the middle section with horses, milk cows and oxen on the one extremity. The family lived mostly on the gable end of the building. The hearth or fireplace was far from the door. The fire was normally made of oak wood and smoke, with no chimney or vent, collected in the middle of the roof and was distributed through the entire structure and finally escaped through the barn door. A reflecting board was placed perpendicular above the fireplace at such a height that it prevented the collecting of the smoke among the beams and rafters by diffusing each column as it rises over the middle region. Dr Cogan compared it to the sounding board on a pulpit.

Some of the Scheuren or Barns had a second small apartment called a stove room. This room was warmed by a stove, or a furnace placed against the wall and generally heated from without through an opening in the partition wall so that the air in the apartment has no access to the fuel but received a close, hot, humid, and unwholesome heat from an accumulation of ignited particles which have no proper vent.

He referred to these machines as ovens. It is a generic term used referring to a particular furnace which is most generally used in Germany at the time. It looks like a furnace! The ovens of the rich were elaborately constructed with an elegantly crafted iron with ornaments and figures in relief with crafted Saxon china. It is useful in large and spacious apartments but in these small spaces, they yield suffocating heat.

To Dr Cogan, this seemed to be the cause for frequent pulmonary complaints in Germany and in England. He mentioned that this is not the case in Holland where rooms are more spacious and fires not so violent and the inhabitants are better dressed for the cold.

The success of the Westphalian hams and bacon was in large part ascribed to the construction of these barns and to the fact that they do not have chimneys. The ham and bacon were hung in the thick stream of smoke, a few yards away from the board by which it was repelled. The fact that it hung in the smoke and not in the heat meant that the fat did not turn rancid as is the case with chimney smoked ham.

Another report points out that if hams are left in a warm and moist environment “they have acquired that degree of softness which precedes purification. Then they are duly salted and exposed to the current [of smoke]. (The Ipswich Journal, 1796) This refers to the curing process but once it has been cured, the meat is hung in the smoke. Curing and smoking are always dealt with in combination and, as we will see later, most often in the context of a very particular brine from Russia called the Impress of Russia’s Brine.

A newspaper report from Northern Ireland in 1841 fills out the picture more fully. It seems that Dr Cogan’s report speaks about small villages. A description comes to us from much earlier, in 1841 and it describes a more “formal” or bigger Westphalia smoking operation. Smoking Westphalia hams was done at this time in “extensive chambers in the upper stories” as Dr Cogan describes, but then seems to be speaking about a structure in a city, either an apartment or large factory because it says that the buildings are “high. . . , some of four or five stories.”

The fire was made in the cellar which also speaks of a bigger building and “the smoke was directed to the meat through pipes in which the heat was absorbed, and the moisture removed.” I would love to know how this was achieved! (Belfast News-Letter, 1841) “The smoke was dry and cool when it came into contact with the meat. The meat is, in this way, perfectly dried and had a flavour and a colour far superior to meat smoked in the “common method.” (Belfast News-Letter, 1841)

The strict aversion to heat of any kind in the smokehouse was not shared universally. Some favoured meat in the drying stage due to the removal of moisture through heat. The Westphalia method of smoking was called “cold smoking” as early as 1864 but there was also a method of smoking called “wet smoke” or “moist smoke” as opposed to “dry smoking”. The complete quote related to Westphalia hams is: “Westphalia Hams. —These usually come by way of Hamburg, and owe their fine flavour to their being “cold smoked.” The hams are hung in the upper part of tin building; the smoke is generated in the cellar and carried up to the smoking-room through tubes. During its ascent, it deposits all moisture, and when it comes in contact with the hams it is both dry and cold so that no undue change occurs in the meat while being smoked. —Newspaper paragraph.” (The English and Australian Cookery Book, 1864)

Revelations by Richard Bradley

Our earliest reference to Westphalia hams and bacon comes through the English botanist, Richard Bradley who sent a letter to James Petiver seeking information on the secret of salting, drying, and blackening bacon, gammon, or ham in the west German way as early as 1714.

The 17th- and early 18th-century methods of preparing these, delicacy eluded him until his great friend John Warner of Rotherhithe went to Germany and wrote him a letter on the subject in about 1721. I quote the entire letter published in 1726.

“Friend Bradley, Thy favour of the 30th ult. I receiv’d; in answer to which, I send thee the method used to cure bacon in and about Hamburgh and Westphalia, which is after this manner: Families that kill one, two, or three hogs a year, have a closet in the garret joining to their chimney, made very right and close, to contain Smoke, in which they hang their Bacon to dry out of the reach of the heat of the fire, that it may be gradually dried by the smoke only, and not by heat; the smoke is conveyed into the closet by a hole in the chimney near the floor, and a place made for an iron stopper to be thrust into the funnel of the chimney about one Foot above the hole, to stop the smoke from ascending up the chimney, and force it through the hole into the closet. The smoke is carried off again by another hole in the funnel of the chimney above the said stopper, almost at the ceiling, where it vents itself. The upper hole must not be too big, because the closet must be always full of smoke, and that from wood fires; for coal, or turf, or peat smoke, I apprehend will not do so well.” (Richard Bradley, 1726)

In terms of curing the meat, the process does not mention the reuse of the old brine which shows that it was not always used in Westphalia. So, even in Westphalia, there were two basic curing methods. One with saltpetre and one where only salt is used. In this instance, the latter is described. John Warner of Rotherhithe writes, “the manner of salting is no other than as we salt meat in common; sometimes they use our Newcastle salt, or St. Ubes, or Lisbon Salt, and a Salt that’s made at Nuremberg (not so good as Newcastle) made from salt springs; in those parts they do not salt their bacon or beef so much as we do in England . . .” (Richard Bradley, 1726)

He quickly returns to the subject and the importance of salt and smoke and shows that in this curing method, no saltpetre is used. In the salt-smoke combination, he focuses again on the smoke. He writes, “the smoke helps to cure, as well as the salt; for I have seen when dry’d flesh hath not hang’d long enough in the smoke, it would be green within, when if it had hung its time, it would have been red quite through; for as the smoke penetrates, it cures the flesh, and colours it red without any salt-petre, or any other Art.” (Richard Bradley, 1726)

The last purported special ingredient in Westphalia ham and bacon is the feed. Some authors try and make a case that they feed their swine differently before they are slaughtered by letting them roam the woods and feed on acorns, but this was also the practice in many parts of England. John Warner of Rotherhithe therefore correctly observes “as to the feed of their swine, I saw no difference between their feed and ours here if any have the preference, I believe the English, and our bacon would be full as good, if not better than the Westphalia if cured alike.” (Richard Bradley, 1726)

He concludes, “I have here above answered thy desire, and wish it may be approved by our Bacon Makers; for the bacon will not only be not so salt, but relish better every way, Thy Friend, John Warner.” (Richard Bradley, 1726)

Transferring the Technology to England

Back to the topic of smoking meat, Bradley gives the most satisfying news that someone in England took him up on his description of the Westphalia smokehouse. First, he thanks his collaborator, Mr Warner for providing him with the information which he was quick to disseminate to interested parties in England. He writes, “I am obliged to Mr John Warner, a very ingenious gentleman of Rotberbith, for the first just account of preparing bacon in the Westphalia manner, and from whose letter to me, I have already communicated to the public the principles of the art.” (Bradley, 1732)

The most satisfying part of the exchange is the report that some took the method up in England. “Since which [the communication to the English public], my learned and curious friend, Dr Corbet of Bourn-Place near Canterbury, has built a bacon-house capable of drying (as I am informed) sixty large hogs at one time, and has even improved upon the Westphalia method, viz. by drying so large a quantity by one fire, when the drying-rooms or closets abroad do not cure, perhaps, above five or fix hogs at a time.” (Bradley, 1732)

The construction in Westphalia smokehouse is the same as we have seen repeatedly, namely a closet that was installed in the attic for ham or bacon smoking. Dr Corbet of Bourn-Place constructed the largest dedicated smokehouse that we are so far aware of in the early 1700s, capable of accommodating 60 large pigs. I assume the Dr Corbett who is referred to and is associated with Bourne-Park, is Dr John Colbert who married the eldest sister of Sir Hewitt, Elisabeth. (Godfrey, 1929) He was not a very savoury character but the fact that he embraces this new method of smoking reveals a positive angle on his character. It may, however, have more to do with him being desperate to fund the large estate than anything else.

Read this fascinating article of how John Corbett gained control over Manor of Bourne, not to any credit of his name. Painting from this article.

Reusing Old Brine

An 1852 report by Youatt makes it clear that the method of reusing old brine and boiling it in between was practised in Westphalia. One cannot take the earlier accounts we looked at as exhaustive and a summary of all the various techniques used in Westphalia. They represent what the reporters saw and none of them set out to do a complete survey of curing and smoking techniques in Westphalia. The account we will look at next is later and may point to a progression in curing techniques of the early 1700s to the early 1800s. On the other hand, it may simply include a method that may have been in use in the early 1700s at certain places and one that the reporters of earlier simply did not see.

It relates to the re-use of the old brine. He writes, “The annexed system is the one usually pursued in Westphalia: — ” Six pounds of rock salt, two pounds of powdered loaf sugar, three ounces of saltpetre, and three gallons of spring or pure water, are boiled together. This should be skimmed when boiling, and when quite cold poured over the meat, every part of which must be covered with this brine. Small pork will be sufficiently cured in four or five days; hams, intended for drying, will be cured in four or five weeks, unless they are very large. This pickle may be used again and again, if it is fresh boiled up each time with a small addition to the ingredients. Before, however, putting the meat into the brine, it must be washed in water, the blood pressed out, and the whole wiped clean.” (Youatt, 1852) This cure was called the Empress of Russia’s Brine.

The Magazine of Domestic Economy, and Family Review, Volume 1, Jan 1843, W.S. Orr & Company gives the same description as Youatt in 1852. The 1843 account begins as follows. “In Europe, the Russian pork is much esteemed, and bears a high price; its quality is supposed to be owin to the pickle in which it is preserved.” The rest of the quote which Youatt omits in his 1852 work reads as follows from 1843: “Pickling tubs should be larger at the bottom than at the top; by which means, when well packed, the pork will retain its place until the last layer is exhausted. When the pork is cool, it may be cut up, the hams and shoulders for bacon, and the remainder salted. Cover the bottom of the tub or barrel with rock-salt, and on it place a layer of meat, and so on till the tub is filled. Use the salt liberally, and fill the barrel with strong brine, boiled and skimmed, and then cooled. The following method of preparing hams and shoulders is a good one, as many who have tried it in substance can testify. To ascertain the probable weight of the meat to be prepared, weigh a number of the hams and shoulders. Then pack them with rock-salt in a suitable tub or cask, being careful not to lay the flat sides of the large pieces upon each other, and filling the intervals with hocks, jowls, & c. To every 300lbs. of meat, then take 20lbs . of rock-salt or Onondaga coarse salt, 1lb. of saltpetre, and 14lbs. of brown sugar, or half a gallon of molasses, and as much water ( pure spring water is the best ) as will cover the meat: put the whole in a clean vessel, boil and scum, then set it aside to cool, and pour it on the meat till the whole is covered some three or four inches. Hams weighing from 12 to 15lbs. must lay in the pickle about five weeks; from 15 to 25lbs. , six weeks; from 25 to 45lbs., seven weeks. On taking them out, soak them in cold water two or three hours to remove the surface salt, then wipe and dry them. It is a good plan in cutting up to take off feet and hocks with a saw instead of an axe, as it leaves a smooth surface and no fractures for the lodgment of the fly. Some make only six pieces of a trimmed hog for salting; but it is more convenient when intended for domestic use, to have the side pork, as it is called, cut in small pieces. The goodness of hams and shoulders, and their preservation, depend greatly on their smoking, as well as salting.”

The Empress of Russia’s Brine

This 1843 report we just looked at and where the brine is described in detail links the Empress of Russia’s brine with Westphalia’s method of smoking. It is not called that specifically, but other sources name the brine. The rest of the quote reads as follows, “The goodness of hams and shoulders, and their preservation, depend greatly on their smoking, as well as salting. Owing to some misconstruction of the smoke house, or to the surface of the meat not being properly freed from the saline matter, or other causes, it not infrequently happens that during the process of smoking, the meat is constantly moist, and imbibes a pyroligneous acid taste and smell, destructive of its good qualities. The requisites of a smoke-house are, that it should be perfectly dry; not warmed by the fire that makes the smoke; so far from the fire, that any vapour thrown off in the smoke may be condensed before reaching the meat; so close as to exclude all flies, mice, & c., and yet capable of ventilation and escape of smoke. The Westphalian hams are the most celebrated in Europe, principally cured at, and exported from, Hamburg. The smoking of these is performed in extensive chambers in the upper stories of high buildings some of four or five stories; and the smoke is conveyed to these rooms from fires in the cellar, through tubes on which the vapour is condensed and heat absorbed, so that the smoke is both dry and cool when it comes in contact with the meat. They are thus perfectly dry and acquire a colour and flavour unknown to those smoked in the common method. Hams after being smoked may be kept any length of time, by being packed in dry ashes, powdered charcoal, or being kept in the smoke-house, if that is secure against the fly, or a smoke is made under them once a week. When meat is fully smoked and dried, it may be kept hung up in a dry room, by slipping over it a cotton bag, the neck of which is closely tied around the string which supports the meat, and thus excludes the bacon bug, & c. The small part of a ham, shoulder, & c., should always be hung downwards in the process of smoking, or when suspended for preservation.”

The main point of this quote above is the date, 1843 where the Empress of Russia’s brine is linked with Westphalia smoking. The brine is also given in the Pictorial Times: Volume 2, Jan 1843. In 1841 in New England Farmer, and Horticultural Register – Volume 19 Joseph Breck and Co. the entire quote is given as I have just given it. Several publications featured the brine in 1839. The Farmers’ Cabinet, Volume 3, 1838 gives the same recipe but says that it was copied from an English publication.

The long version of the recipe also appeared in a number of newspapers at that time. New England Farmer, 1841 is one example. Several more carried it between 1842 and 1844. Of great interest is the same report that appeared in the Belfast News-Letter, 1841. The name of the brine is given as the Empress of Russia’s Brine.

Who was the Empress?

– Alexandra Feodorovna?

So, the origin of the cure is Russian, but who will the Empress be that is referring to. I asked the question on a Russian site and Maria Didurenko responded almost immediately. “At that time, the Empress was Alexandra Feodorovna, the wife of Nicholay the First. She was of Prussian origin and according to my information, which, perhaps, colleagues will correct, she was not fond of gastronomy at all. Salt was relatively expensive at that time, the cost of a pood of salt (16 kg) was about 300 silver rubles (source General I. F. Blaramberg). I can assume that it was the high cost that made it necessary to look for options for the most efficient use of expensive raw materials.”

The first option I have is then Alexandra Feodorovna, born Princess Charlotte of Prussia, the wife of Nicholay the First. Without any reason to doubt the veracity of the information given me I wondered if there was another Empress of Russia who was closely associated with salt. From the references we looked at so far, it seems unlikely that she is the empress referred to since she passed away in 1860 and the 1810 reference to the brine which we will look at momentarily, refers to her as already “late” by 1810. It, therefore, ruled out Alexandra Feodorovna.

More importantly than the actual name that Maria Didurenko gave me “what to look for!” She started a twofold quest. On the one hand, to see if I can find a name associated with the reference in any of the many references to this brine and on the other hand, can I identify an Empress of Russia who was deeply involved in salt?

– A clue – Catherine?

Baylor (1889) offers a further clue when he writes, about an “Incomparable Method of Salting Meat as Adopted by the late Empress of Russia,” “more expensive than common brine,” as imperial brine has a right to be, “but promising advantages that most people would be glad to purchase at a much higher price.” It seemed as if the phrase, “Incomparable Method of Salting Meat as Adopted by the late Empress of Russia,” was a heading for the discussion on the brine and the reference to it as the “Empress of Russia’s Brine” to be a change that was later made. So, when I searched for the more likely original title, I happened upon the 1810 publication, The Family Receipt-book, Or, Universal Repository of Useful Knowledge and Experience in All the Various Branches of Domestic Economy, Oddy and Company. This publication gives the same Empress of Russia’s Brine, with the phrase, “Incomparable Method of Salting Meat as Adopted by the late Empress of Russia” as the heading, just as I suspected it would be but adds the following sentence, “the following method of salting meat is asserted to have been used by the great Empress Catharine, in her household establishment, with the utmost success.”

Before we look at the identity of the Empress in question, first a look at additional information given about the brine in what is most likely the original quote. The wording is slightly different and other elements are discussed. It begins the same way. “Boil together, over a gentle fire, six pounds of common salt, two pounds of powdered loaf sugar, three ounces of saltpetre, and three gallons of spring water. Carefully scum it, while boiling; and, when quite cold, pour it over the meat, every part of which must be covered with the brine .”

The fact that it is intended to be used again only becomes clear towards the end of the quote. The following is what is omitted by the other references. “In this pickle, it is said, the meat will not only keep for many months, but the hardest and toughest beef will thus be rendered as mellow and tender as the flesh of a young fowl; while either beef, pork, or even mutton, will have a fine flavour imparted by it. In warm weather, however, the blood must be expressed from the meat, and the whole well rubbed over with fine salt before it is immersed in the liquor. Young pork should not be left longer than three or four days in this pickle, as it will then be quite sufficiently softened: but hams, intended for drying, may remain a fortnight before they are hung up; when they should be rubbed with pollard, and closely covered with paper bags, to prevent their being fly-blown. Though this pickle is, at first, somewhat more expensive than common brine, as it may be again used, on being boiled with additional water and the other ingredients, it is far from being, on the whole, importantly more dear; while it seems to promise advantages which most people would be happy to purchase at a much higher price.”

The enigmatic phrase “it seems to promise advantages which most people would be happy to purchase at a much higher price” without question refers to the speed of curing. The phrase “with advantage” has also cropped up in other references to the re-use of brine and I wonder if those references are not all based on this one from the brine of Catherine!

The link which other authors make between the Empress of Russia’s Brine and Westphalian hams and bacon is almost certainly a later addition, a link that did not originally exist. It is quite possible that due to the reference we have of the re-use of the brine in Westphalia, that this region became one of the earliest to adopt the “Empress Brine” outside Russia and the link between the two may be as simple as this. The original method used in Westphalia was described in the same terms as the “Empress Brine.”

– Catherine the Great!

Catherine, who is referred to, was most certainly non-other than Catherine II (born Sophie of Anhalt-Zerbst; 2 May 1729 – 17 November 1796), most commonly known as Catherine the Great. She was the last reigning Empress Regnant of Russia (from 1762 until 1796) and the country’s longest-ruling female leader.

The Belfast News-Letter (Belfast, Antrim, Northern Ireland), 26 Oct 1841 now becomes important. If this brine was discovered by Catherine the Great, or someone associated with her court, and if the reports of the brine made it to Antrim, Northern Ireland much earlier than 1841, then the tantalising possibility exists that William Oake, the chemist from Ulster in Northern Ireland, learned of the existence of this brine and progressed the idea by doing away with the boiling step between the different batches. The earliest mention of mild cured bacon I could find was in newspaper reports from Antrim, Northern Ireland in 1837. It is fair to conjecture that the invention did not happen far from there. The report that William Oake from Ulster invented the process and the earliest reference to “mild cured bacon” coming from Antrim correlates since Antrim is in Ulster. The fact that the existence of the Empress of Russia’s brine was reported on, four years later, also in Antrim, seems to be too much to be merely coincidental!

Of all the Empresses of Russia, Catherine the Great fits the profile of the inspiration behind the brine or possibly its inventor, the best. It was in her time that the salt tax would play a major part in Russian society. By the end of the 1760s, the combined direct taxes, the salt tax with the liquor tax would account for more than 3/4 of the national income in a time when the Russian economy was desperate for revenue to fund its expansions. (LeDonne, 1975)

The person behind the drive to raise indirect taxes was Petr Ivanovič Šuvalov, the chief of the artillery. His thinking dominated policy in the 1750s to the extent that he was in reality the minister of the economy. Collecting the indirect taxes amongst which salt was a major component was so successful that between 1750 and 1756 he was able to reduce direct taxes. (LeDonne, 1975)

The first expression of Petr Ivanovič Šuvalov’s new policy was then a steep increase in the price of salt. “In January 1750 the price of a pud of salt was raised from about 21 kopeks to 35 kopeks and in August 1756, at the outset of the Seven Years’ War, to 50 kopeks. This was a dangerous expedient and it backfired in the form of reduced consumption and increased smuggling. . . Salt became out of reach for so many that one of the first acts of Catherine was to reduce the price by 20% to 40 kopeks in July 1762.” (LeDonne, 1975)

“The second component of Suvalov’s policy was to open up new and possibly cheaper sources of salt. The production of Perm (Solikamsk) salt could not be raised beyond a certain level because it depended on the availability of labor, the supply of wood fuel, and the length of the work season. In the late 1740s the state began the exploitation of Ileck rock salt and, more important, the extraction of salt from Lake EPton. Transportation costs, however, were so great, resulting in part from the insecurity of the trans-Volga region, that these salts could only supplement Perm salt, not replace it. The result of this increased production was the closing of older but uneconomical sources, at Bachmut, Staraja Russa, Balachna and Soligalic.” (LeDonne, 1975)

Suvalov’s policy only created an ambiguous situation because it rested on a contradiction: raising the price of salt cancelled part of the benefits that could be expected from the rise in supply. Catherine’s policy was wiser. It combined a cut in prices with a major effort to develop production, and it resulted in making salt available everywhere at a reasonable price. During the first decade of her reign, however, little was done beyond reducing the price of salt. This, however, shows us that she was deeply aware of the suffering that the salt tax caused and she was actively involved in finding ways to reduce the cost of salt. It is perfectly in step with the invention of a way to recover salt that would be lost if the old brine is discarded.

“A commission of three members under general Fermor was set up in 1764 to make a thorough examination of the salt trade and to recommend measures to remove widespread abuses. It was closed in 1768 and its work left little mark on legislation. In 1771 the president of the College of Audit was transferred to the Main Salt Board ostensibly to remedy a chaotic situation. It was decided in 1772 to reorganize the Board, to require it to purchase enough salt to have a permanent two-year reserve always available, and to improve the accounting of procedures. Four years later, however, a major reform of local government began to take effect and the salt administration was integrated into the new structure. This was the purpose of the code of 1781.” (LeDonne, 1975)

For the full treatise on the salt tax in Catherine’s Russia and the salt code of 1781 by John P. LeDonne, see “Further Reading.

Salt was a key commodity in the world of Catherine the Great! One of the uses was in curing meat. For Catherine to suggest the boiling of the brine as a way of “cleaning” it so that it can be re-used was a stroke of genius. I refer you to the production method of one of the major sources of salt in Russia namely that of Penn salt. It was produced exclusively from natural brines. “Production techniques were relatively simple, but they required careful supervision and consumed large quantities of firewood. It was first necessary to pump up the brackish water to the surface or, in favourable circumstances, to tap an artesian source. The next step was to remove the suspended impurities and to increase the salinity of the solution – even a rich natural brine might include but three percent salt – by exposing it to the sun so as to cause evaporation. This was done by various methods, their chief purpose being to create maximum exposure and ventilation.” (LeDonne, 1975)

“The brine was then poured into large horizontal pans [creny] under which a fire was kept going without interruption. The brine was brought to the boiling point and kept boiling for several hours. Impurities sank to the bottom or rose to the surface and were removed with a long hoe-like instrument called a kocerga. Then precipitation began. Heat was reduced and when little of the mother-liquor remained the salt was raked away. Boiling down the brine took about six hours, and the precipitation lasted from half a day to three days depending on the desired grain of salt.” (LeDonne, 1975)

There may have been another reason for boiling it which is at first not all that obvious. I found many of the references specifying the use of rock salt. Let’s return to LeDonne (1975). He writes, “At the southern end of the Ural range, sixty versts south from Orenburg, exploitation by the state of a huge underground salt dome began in 1754 near the Ilek river. Rock salt is of lesser quality than salt obtained by boiling – it dissolves more slowly and is never free from impurities -but it is easier to obtain. Petr Ivanovic Ryckov, who became the administrator of the mine in 1770, pronounced it so pure that it could not be distinguished from sugar, although the Salt Board in Moscow was of a different opinion. The Board was probably right because rock salt strata are usually interbedded with thin layers of gypsum. The salt was extracted in the form of large blocks weighing thirty to forty puds (since 1899, set at approximately 16.38 kilograms or 36.11 pounds), then broken up with hammers. In such blocks a “heart” was sometimes found as pure and clear as crystal. But salt dust often became mixed with dirt and sand on the way to the stores and this lowered its general quality.” (LeDonne, 1975) Boiling the brine would therefore have been a very good idea, nevertheless, even before any curing is attempted. This may be a reason for heating salt in a pan before it is rubbed into the meat, as was commonly practised, even where dry salting is used and not a liquid brine. The fact that heat was used to “clean brine” was a well-known practice. The progression was the boiling of the used brine.

There is a problem with this theory though in the context of the Empress of Russia’s brine. The first brine batch was not boiled! The technique of boiling the salt was a known technology but it was not used to concentrate the salt as was the case in salt recovery and if the purpose were sterilizing the salt, it would have been done for the first brine batch also. Considering the knowledge of microorganisms during the time of Catherine the Great, my suspicion is that decay through microorganisms was associated with meat and not with salt. I suspect that in their view, the brine was “contaminated” only after it encountered the meat. I developed this thought in detail in my article, “The Mother Brine.”

A comment is in order as to the relationship between the Empress of Russia’s Brine and the smoking of Westphalia Hams. If it is true that salt was in short supply, it would have been doubly so for saltpetre. It warrants careful future study, but the fact that saltpetre was omitted from some of the cures in Westphalia could almost certainly be ascribed to the scarcity of this resource. So, saltpetre was scarse in Russia. Westphalia learned how to cure meat with smoke only with salt – no saltpetre. That Russians adopted the Westphalian smoking techniques, and that Westphalia adopted the Empress of Russia’s salt recovery technology stands to reason! That they witnessed extraordinary value in a salt/ saltpetre brine that is re-used both in Russia and Westphalia is a deduction that flows from the facts!


The fact that William Oake is the inventor of the mild curing system that developed into tank curing is by now a well-established fact. (Mild Cured Bacon) His inspiration to re-use the old brine could very likely have come from this Russian invention under Catherine the Great! The link with the smoking technology of Westphalia is fascinating and that cross-pollination took place between these two curing-superpowers stands to reason. The impetus of the invention was the salt tax and the actions of Petr Ivanovič Šuvalov and Catherine the Great’s desire to mitigate the effect of these measures on the Russian curers.

The world has seen two major movements to facilitate the curing with nitrite salts. One was this one. The method is indirect and came about almost by accident. Russian technology that became known in Ireland which, in the hands of a chemist, became tank curing. Nitrite formation through fermentation.

The second major development was caused by the First World War when the use of nitrates was restricted for the war effort, resulting in the use of nitrite salts directly. (The Direct Addition of Nitrites to Curing Brines – the Master Butcher from Prague and The Direct Addition of Nitrites to Curing Brines – The Spoils of War)

(c) Eben van Tonder

Westphalia Bacon Recipes

Westphalian Hams and Bacon Recipes

Further Reading

The Mother Brine

Chapter 09.01 – Mild Cured Bacon

Chapter 11.04: Wiltshire Cured or Tank Cured Bacon

Tank Curing Came From Ireland

Westphalia Bacon and Ham & the Empress of Russia’s Brine: Pre-cursers to Mild Cured Bacon

Meat Curing – A Review

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Baylor, F. C., 1889, A Shocking Example, and Other Sketches, J. B. Lippincott

Belfast News-Letter (Belfast, Antrim, Northern Ireland), 26 Oct 1841, Tue

Bradley, R.. 1726. A General Treatise of Husbandry and Gardening. T Woodward.

The Family Receipt-book, Or, Universal Repository of Useful Knowledge and Experience in All the Various Branches of Domestic Economy, Oddy and Company, 1810

Godfrey, W. H., F.S.A., F.R.I.B.A. Bour Park, Near Canterbury. Archeological Constantia, Vol 41, 1929

The Ipswich Journal (Ipswich, Suffolk, England), 19 Mar 1796, Sat

LeDonne, J. P. (1975). Indirect Taxes in Catherine’s Russia I. The Salt Code of 1781Jahrbücher Für Geschichte Osteuropas23(2), 161–190.

The Magazine of Domestic Economy, and Family Review, Volume 1, Jan 1843, W.S. Orr & Company

New England Farmer, and Horticultural Register – Volume 19 Joseph Breck and Co. 1841.

New England Farmer (Boston, Massachusetts), 13 Jan 1841, Wed.

Pictorial Times: Volume 2, Jan 1843

The Farmers’ Cabinet, Volume 3, 1838

Youatt, W. 1852. The pig: a treatise on the breeds, management, feeding, and medical treatment, of swine; with directions for salting pork, and curing bacon and hams. New York, C. M. Saxton