Soya: Review of some health concerns and applications in the meat industry


Vagadia et al. (2015) state that soya “contains a variety of bioactive anti-nutritional compounds including protease trypsin inhibitors, phytic acid, and isoflavones that exhibit undesirable physiological effects and impede their nutritional quality. Inactivation of these trypsin inhibitors, along with deleterious enzymes, microbes, bioactive components and increasing the protein quality by improving its texture, colour, flavour, functionality and digestibility are the most important factors to be considered in the crucial stage in the manufacturing of soy products.”  Are there reasons to be concerned and what can we learn about its history and possible applications in the meat industry?

Historically Valued Plant

Before we break down the concerns raised by Vagadia et al. (2015), it is instructive to know that soya has been consumed in many countries since before recorded history.  A rich tradition developed around its use in medicine from antiquity.    Duke (1991) showed that a search of his “Medicinal Plants of the World” database (Sept. 1981) indicated that soybeans are or have been used medicinally in China to treat the following symptoms/diseases or for the following medicinal properties (listed alphabetically; Most information from: Li Shih-Chen. 1973. Chinese Medicinal Herbs. San Francisco: Georgetown Press):

“Abortion, ague, alcoholism, anodyne, antidote for aconite or centipede or croton, antivinous, anus, apertif, ascites, ataxia, blindness, bone, bugbite, burn, carminative, chestcold, chill, circulation, cold, complexion, decongestant, diaphoretic, diuretic, dogbite, dysentery, dyspnea, eczema, edema, enuresis, feet, fever, halitosis, headache, hematuria, impotence, intoxication, kidney, labor, laxative, leprosy, malaria, marasmus, marrow, melancholy, metrorrhagia, nausea, nervine, ophthalmia, pile, pregnancy, preventive (abortion) puerperium, refrigerant, resolvent, rheumatism, scald, sedative, skin, smallpox, snakebite, sore, splenitis, splinter, stomach, tinea, venereal, vertigo, vision.”

Uses in other parts of the world include cancer, and cyanogenetic, shampoo (USA), diabetes (Turkey), soap (Asia), stomach problems (India).

Not only was it recognized as a superfood in many parts of the world, but it was celebrated for its medicinal value.  Looking at the factors of concern raised by many, we begin by looking at the most well-known concern factor of its role as a trypsin inhibitor.

Trypsin Inhibitors

The German physiologist Wilhelm Kühne (1837-1900) discovered trypsin in 1876. It is an enzyme that cleaves peptide bonds in proteins (serine protease) and is therefore essential in digestion.   It is found in the digestive system of many vertebrates, where it hydrolyzes proteins. (Kühne, 1877)  Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen, produced by the pancreas, is activated. (Engelking, 2015)  A trypsin inhibitor (TI) is then something (a protein) that reduces the biological activity of trypsin and as such have a negative effect on nutrition by impairing the digestion of food.

The concern about soya’s trypsin inhibitors is of no real concern to us.  It turns out that trypsin in humans is more resistant to inhibition than is the trypsin of other mammalian species. “The effect on human trypsin of soybean trypsin inhibition in soy protein does not appear to be a potential hazard to man. Therefore, the elimination of STI does not seem to be necessary for humans.”  (Flavin DF, 1982)

“In animal diets, however, pancreatic toxicity must be considered whenever soybean protein is utilized. Soybeans should be treated to increase their nutritional benefits and decrease any animal health risks. This will ensure healthy control subjects in laboratory situations and avoid misinterpretation of pathologic data.

The treatment suggested is heat since heat will destroy most of the soybean trypsin inhibitors. Additional supplementation is required following heat treatment for amino acids such as methionine, valine, and threonine; for choline; and for the minerals zinc and calcium.  Excessive heat must be avoided since it will decrease the nutritional value of soybean protein and increase lysinoalanine, a nephrotoxic substance.

Finally, the use of STI as a promotor in the study of potential pancreatic carcinogens may prove beneficial for cancer research and might be considered in the future.” (Flavin DF, 1982)

Phytic acid

Phytic acid also is suspect due to its inhibitory effect related to nutrition.  Anderson (2018) states “It is a unique natural substance found in plant seeds. It has received considerable attention due to its effects on mineral absorption. Phytic acid impairs the absorption of iron, zinc, and calcium and may promote mineral deficiencies”  (Arnarson, 2018)

As is the case with the trypsin inhibition, the story is a bit more complicated than that because phytic acid also has a number of health benefits.

Anderson writes that “phytic acid, or phytate, is found in plant seeds. It serves as the main storage form of phosphorus in the seeds. When seeds sprout, phytate is degraded and the phosphorus released to be used by the young plant. Phytic acid is also known as inositol hexaphosphate, or IP6. It’s often used commercially as a preservative due to its antioxidant properties.

Phytic acid is only found in plant-derived foods. All edible seeds, grains, legumes and nuts contain it in varying quantities, and small amounts are also found in roots and tubers. The following table shows the amount contained in a few high-phytate foods, as a percentage of dry weight:

Phytic Acid in food

As you can see, the phytic acid content is highly variable. For example, the amount contained in almonds can vary up to 20-fold.

Phytic acid impairs absorption of iron and zinc, and to a lesser extent calcium.  This applies to a single meal, not overall nutrient absorption throughout the day.  In other words, phytic acid reduces mineral absorption during the meal but doesn’t have any effect on subsequent meals.  For example, snacking on nuts between meals could reduce the amount of iron, zinc and calcium you absorb from these nuts but not from the meal you eat a few hours later.

However, when you eat high-phytate foods with most of your meals, mineral deficiencies may develop over time.  This is rarely a concern for those who follow well-balanced diets but may be a significant problem during periods of malnutrition and in developing countries where the main food source is grains or legumes.

Avoiding all foods that contain phytic acid is a bad idea because many of them are healthy and nutritious.  Also, in many developing countries, food is scarce and people need to rely on grains and legumes as their main dietary staples.

Phytic acid is a good example of a nutrient that is both good and bad, depending on the circumstances.  For most people, it’s a healthy plant compound. Not only is phytic acid an antioxidant, but it may also be protective against kidney stones and cancer.  Scientists have even suggested that phytic acid may be part of the reason why whole grains have been linked with a reduced risk of colon cancer.

Phytic acid is not a health concern for those who follow a balanced diet.  However, those at risk of an iron or zinc deficiency should diversify their diets and not include high-phytate foods in all meals.  This may be especially important for those with an iron deficiency, as well as vegetarians and vegans.

There are two types of iron in foods: heme iron and non-heme iron.  Heme-iron is found in animal foods, such as meat, whereas non-heme iron comes from plants.

Non-heme iron from plant-derived foods is poorly absorbed, while the absorption of heme-iron is efficient. Non-heme iron is also highly affected by phytic acid, whereas heme-iron is not.  In addition, zinc is well absorbed from meat, even in the presence of phytic acid.

Therefore, mineral deficiencies caused by phytic acid are rarely a concern among meat-eaters.  However, phytic acid can be a significant problem when diets are largely composed of high-phytate foods while at the same time low in meat or other animal-derived products.  This is of particular concern in many developing nations where whole grain cereals and legumes are a large part of the diet.”  (Arnarson, 2018)


Isoflavones are a class of phytoestrogens — plant-derived compounds with estrogenic activity. Soybeans and soy products are the richest sources of isoflavones in the human diet.  (

“Since many breast cancers need estrogen to grow, it would stand to reason that soy could increase breast cancer risk. However, this isn’t the case in most studies.

In a review of 35 studies on soy isoflavone intake and breast cancer incidence, higher soy intake reduced breast cancer risk in both pre- and postmenopausal Asian women.  For women in Western countries, one study showed soy intake had no effect on the risk of developing breast cancer.

This difference may be due to the different types of soy eaten in the Asian compared to the Western diet. Soy is typically consumed whole or fermented in Asian diets, whereas in Western countries, soy is mostly processed or in supplement form.

In an animal study, rats fed fermented soy milk were 20% less likely to develop breast cancer than rats not receiving this type of food. Rats fed soy isoflavones were 10–13% less likely to develop breast cancer.  Therefore, fermented soy may have a more protective effect against breast cancer compared to soy supplements.  Additionally, soy has been linked to a longer lifespan after breast cancer diagnosis.

In a review of five long-term studies, women who ate soy after diagnosis were 21% less likely to have a recurrence of cancer and 15% less likely to die than women who avoided soy.”  (Groves, 2018)

From the above notes, it may appear that it is perfectly safe for humans to consume raw soya.  There is however one very good reason to cook soya well before it is consumed.

Lectin Effects

“Soybeans contain lectins, glycoproteins that bind to carbohydrates in cells. This can damage the cells or lead to cell death in the gastrointestinal tract. Lectins may bind to the intestinal walls, damaging the cells and affecting nutrient absorption as well as causing short-term gastrointestinal side effects. Unlike most proteins, lectins aren’t broken down by enzymes in the intestine, so the body can’t use them. Lectins can affect the normal balance of bacteria in the intestine and the immune system in the digestive tract.” (Perkins, 2018)

Dr. Mark Messina discussed the issue with Lectin in soya in a brilliant article entitled “Is Soybean Lectin an Issue?”  He writes, “Given all the attention they’re receiving, you might think these proteins are newly discovered, perhaps because of a sudden advance in technology. Given all the concerns being raised about them, you might be thinking of avoiding foods that contain them. If you do, you can pretty much say goodbye to a long list of healthy foods such as legumes (including soy and peanuts), eggplant, peppers, potatoes, tomatoes, and avocados. Despite the hoopla, studies show there is little reason for concern.

Lectins are anything but new to the scientific community. They are a class of protein that occurs widely in nature and have been known to exist in plants for more than a century. Much of the lectin research has focused on legume lectins but these carbohydrate-binding proteins are widely distributed throughout the plant kingdom. The lectin in soybeans was discovered in the 1950s.

In plants, lectins appear to function as nitrogen storage compounds, but also have a defensive role, protecting the plant against pests and predators. They are capable of specific recognition of and binding to carbohydrate ligands. The term lectin (legere = Latin verb for to select) was coined by Boyd circa 1950 to emphasize the ability of some hemagglutinins (lectins) to discriminate blood cells within the ABO blood group system.5-The term lectin is preferred over that of hemagglutinin and is broadly employed to denote “all plant proteins possessing at least one non-catalytic domain, which binds reversibly to a specific mono- or oligosaccharide.”

Orally ingested plant lectins remaining at least partially undigested in the gut may bind to a wide variety of cell membranes and glycoconjugates of the intestinal and colonic mucosa leading to various deleterious effects on the mucosa itself as well as on the intestinal bacterial flora and other inner organs. The severity of these adverse effects may depend upon the gut region to which the lectin binds. Several cases of lectin poisoning due to the consumption of raw or improperly processed kidney beans have been reported.

The lectin content of soybeans varies considerably among varieties, as much as fivefold. However, from a nutritional perspective, it is the amount in properly processed soyfoods that is most relevant. Although there has been a lot of debate about whether even active soybean lectin is harmful,  a true pioneer in this field, Irvin E. Liener, concluded that soybean lectin isn’t a concern because it is readily inactivated by pepsin and the hydrolases of the brush border membrane of the intestine. But, others think soybean lectin does survive passage through the small intestine.

Not surprisingly, autoclaving legumes including soybeans completely inactivates lectins. However, foods aren’t typically autoclaved. The most practical, effective, and commonly used method to abolish lectin activity is aqueous heat treatment. Under conditions where the seeds are first fully soaked in water and then heated in water at or close to 100°C, the lectin activity in fully hydrated soybeans, kidney beans, faba beans, and lupin seeds is completely eliminated.  Thompson et al. noted that cooking beans to the point where they might be considered edible are more than sufficient to destroy virtually all of the hemagglutinating activity of lectins. More recently, Shi and colleagues23 found that soaking and cooking soybeans destroyed more than 99.6% of the lectin content, which agrees with earlier work by Paredes-Lopez and Harry.

Finally, evidence from clinical trials in no way suggests that the possible residual lectin content of soyfoods is a cause for concern. Adverse effects typically associated with lectin toxicity don’t show up in the hundreds of clinical trials involving a range of soy products that have been published. Not surprisingly, the U.S. Food and Drug Administration recently concluded that soy protein is safe.”  (Messina, 2018)

Saponins in Soybeans

Saponins in soya are responsible for the bitter taste, foam-forming, and activities that rupture or destroy red blood cells.  Its presence in soya is probably an evolutionary development to protect it against, for example, Callosobruchus chinensis L., a common species of beetle.  Its protecting properties can be seen for example by the fact that [certain strains of] the first instar larvae, after burrowing beneath the seed coat, subsequently die without moulting. (Applebaum, 1965)

There are five known soya saponins: Soya sapogenols A, B, C, D, and E.  Saponins cannot be inactivated by cooking because cooking doesn’t break down this toxin like it does lectins.”  (Perkins, 2018)  “Triterpenoid saponins in the mature soybean are divided into two groups; group A soy saponins have undesirable astringent taste, and group B soy saponins have health-promoting properties. Group A soy saponins are found only in soybean hypocotyls, while group B soy saponins are widely distributed in legume seeds in both hypocotyls (germ) and cotyledons. Saponin concentrations in soybean seed are ranged from 0.5 to 6.5%.”  (Hassan, 2013)

Bondi and Birk (1966) investigated soybean saponins as related to the processing of petroleum etherextracted meal for feed and to the preparation of soy foods.  They found that “soybean saponins are harmless when ingested by chicks, rats and mice even in a roughly threefold concentration of that in a 50% soybean meal supplemented diet.” They are decomposed by the caecal microflora of these 3 species. Their non-specific inhibition of certain digestive enzymes and cholinesterase is counteracted by proteins which are present in any natural environment of these saponins. The haemolytic activity of soybean saponins on red blood cells is fully inhibited by plasma and its constituents –
which naturally accompany red cells in blood. Soybean saponins and sapogenins are not absorbed into the blood-stream (Note: Or perhaps not observed in the bloodstream). It may, therefore, be concluded that haemolysis – one of the most significant in vitro [in glass/test tubes] properties of soybean saponins and others–bears no ‘obligation’ for
detrimental activity in vivo [in living organisms].”  (Bondi, et al, 1966)

Birk, et al, 1980, found that “saponins are glycosides that occur in a wide variety of plants. They are generally characterized by their bitter taste, foaming in aqueous solutions, and their ability to hemolyze [break down] red blood cells. The saponins are
highly toxic to cold-blooded animals, their toxicity being related to their activity in lowering surface tension. They are commonly isolated by extraction of the plant material with hot water or ethanol.”  (Birk, 1980)  Leaching the saponins out of the soybeans, removing the bitter taste.  (Perkins, 2018)

Applications and History

Reviewing the history of the development of soya industry in Israel, brought up some interesting perspective on its application in food.

“Hayes Ashdod was one of Israel’s first company to make foods from soybeans and Israel’s first manufacturer of modern soy protein products. In 1963 the company launched its first product, a soy protein concentrate named Haypro. This product was also the first commercial soy protein concentrate manufactured outside the United States. The main applications for Haypro were as a meat extender.”  (Chajuss, 2005)

“In 1966 Hayes Ashdod Ltd. introduced texturized soya protein concentrates under the brand names Hayprotex and Contex. Hayprotex was designed for use mainly as a minced
meat extender, while Contex was designed mainly for vegetarian analogs.”  (Chajuss, 2005)

“Concerning early textured soy protein concentrates: Hayes Ashdod introduced Hayprotex and Contex in 1966, and a company we are well familiar with for making nitrite curing of meat commercially available around the world through their legendary Prague Powder, the Griffith Laboratories from Chicago introduced GL-219 and GL-9921 in 1974, and Central Soya introduced Response in 1975.”  (Chajuss, 2005)

“In 1969 Hayes started to produce Primepro, a more functional and soluble soy protein concentrate, by further treatment of the aqueous alcohol extracted soy protein concentrate (Haypro), for use as substitutes for soy protein isolates and for caseinates in various food systems, especially in the meat processing industries.”  (Chajuss, 2005)

Further reading

A tremendous resource on research on soya is HISTORY OF SOYBEANS AND SOYFOODS IN THE MIDDLE EAST


Soya is a tremendous food and protein source.  The health concerns are addressed at the manufacturing stage.  Application of isolates, concentrates and TVP are multiple.  Even today, after being available on the market for so many years, all its various applications in foods have not been exhausted.  We are limited only by our imagination and interesting work remains to integrate its use into modern meat processing plants.


Applebaum, S.W.; Gestetner, B.; Birk, Y. 1965.  Physiological aspects of host specificity in the Bruchidae–IV.  Developmental incompatibility of soybeans for Callosobruchus. J. of Insect Physiology 11(5):611-16. May.

Arnarson, A.  2018. Phytic Acid 101: Everything You Need to Know.

Birk, Yehudith; Peri, Irena. 1980. Saponins. In: I.E. Liener, ed. 1980. Toxic Constituents of Plant Foodstuffs. 2nd ed. New York: Academic Press. xiv + 502 p. See p. 161-182. Chap. 6.

Bondi, A.; Birk, A. 1966. Investigation of soybean saponins as related to the processing of petroleum ether-extracted meal for feed and to the preparation of soy foods, to provide information basic to improving the nutritional value of soybean protein products. Rehovot, Israel: Hebrew University. 80 + xvii p. USDA P.L. 480. Project no. UR-A10-(40)-18. Grant no. FG-IS-112. Report period 1 March 1961 to 28 Feb. 1966. Undated. 28 cm.

Chajuss, D.. 2005. Brief biography and history of his work with soy in the USA and Israel. Part II (Interview). SoyaScan Notes. Feb. 19. Followed by numerous e-mails. Conducted by William Shurtleff of Soyfoods Center.

Duke, J. A. 1991. Research on biologically active phytochemicals in soybeans (Interview). SoyaScan Notes. Oct. Conducted by William Shurtleff of Soyfoods Center.

Engelking, Larry R. (2015-01-01). Textbook of Veterinary Physiological Chemistry (Third Edition). Boston: Academic Press. pp. 39–44. ISBN 9780123919090.

Flavin DF. The effects of soybean trypsin inhibitors on the pancreas of animals and man: a review. Review article. Vet Hum Toxicol. 1982. 1982 Feb;24(1):25-8.

Groves, M..  2018.  Is Soy Good or Bad for Your Health?

Hassan, S. M..  2013.  Soybean, Nutrition, and Health.  Intech

Kühne, W. 1877. “Über das Trypsin (Enzym des Pankreas)”, Verhandlungen des naturhistorisch-medicinischen Vereins zu Heidelberg, new series, vol. 1, no. 3, pages 194-198

Messina, M.  2018.  Is Soybean Lectin an Issue?  The Soy Nutrition Institute
The latest findings in soy health research,

Perkins, S.  2018. What Happens if You Eat Raw Soybeans?

Vagadia, B. H., Vanga, S. K., Raghavan, V. 2015.  Inactivation methods of soybean trypsin inhibitor – A review. Received 14 December 2015, Revised 21 January 2017, Accepted 19 February 2017, Available online 27 February 2017. Elsevier. Trends in Food Science & Technology, Volume 64, June 2017, Pages 115-125

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