Creating the Optimal Frankfurter Style Sausage in Africa: Hungarians and Russians
by Eben van Tonder
27 November 2021
Over the years I have written about the history of the development of Russian sausages in South Africa (Origins of the South African Sausage, Called a Russian). I’ve created poems about it! 🙂 (Ode to the Russian Sausage – a Technical Evaluation) It is a South African frankfurter style sausages. In Australia, it is called a Kransky and in Zambia and parts of the DRC, it is called a Hungarian. A Hungarian is made without showpieces which means that the exact same product in South Africa is called a smokey or a penny polony. The basic formulations are, however, the same. It is a fine emulsion sausage.
I have looked at every aspect of Russian/ Hungarian making except cooking/ smoking and packing it. This week attention shifted to these final aspects. Daniel Erdei from the smokehouse producer Kerres visited me in South Africa. Their new hybrid smoke system, combining vertical and horizontal airflow systems make them, in my opinion, the best option in the world. They claim a reduction of 30% in cooking/ smoking loss.
Apart from smoking/ cooking, I looked at packaging with shelf life in mind. Many of the large producers in South Africa opted for High-Pressure Pastorisation over the last few years following the Listeriosis epidemy. It is an extremely expensive solution, and I was keen to see what else is on the market.
In South Africa there are several producers who manufacture between 60 and 100 tons of these sausages per day and the economic benefit of this consideration can hardly be overrated. Besides these, current projects underway in other African countries will soon see the same production levels from other African regions. This, coupled with the devastating effects of Covid on international food prices makes the work urgent.
The danger and impact of Covid were highlighted to us while we were in Simons Town, at the famous Brass Bell-Inn and Daniel, a German citizen, started getting calls from family and from the management at Kerres as they were scrambling to get him on the first available flight out of South Africa after the discovery of a new Omicron variant (Variant B.1.1.529) and as countries from around the world were announcing the immediate cancellation of flights from and into South Africa.
After the logistics were arranged and we were satisfied that the best measures were taken to ensure his speedy return to Germany, we continued with our adventure while designing the optimal Russian/ Hungarian line and processing approach.
The following discussion points were all highlighted and interrogated yesterday.
Novel Processing Techniques
– DCD Technology from Green Cell
Work done with DCD Technology (The Power of Microparticles: Disruptor (DCD) Technology) shows the feasibility to use nutritious parts of an animal carcass previously not included in raw material for such sausages. DCD has proven to be extremely important even though it was shown to be less effective in certain specific areas of application (Muscle Structure (Biology)). For large throughput factories it, however, is an ideal solution to increase the overall digestibility of certain raw materials since digestibility is closely related to comminution (Notes on Comminution and Digestibility). It also offers a way to apply pressure for micro control in a way that was previously only possible with HPP or similar systems (for example pulse technology). Two years of intensive work showed that DCD technology has a definite place in meat processing. A proper understanding of its strengths and weaknesses, along with alternative processing techniques that we developed for certain areas of application allows us to create our own MDM/ MSM. MDM or MSM is widely used in Africa as the basis for these sausages (MDM – Not all are created equal!). The MDM-replacer we created has been shown to be more nutritious compared to MDM, imported from, for example, South America and has greater functionality than using MDM alone.
– Binding of water
Water act as the plasticizer in the system. The meat’s texture in these sausages “is due to its property of heat-induced long-chain gelling or setting” and the “cooked meat is classifiable as a water-plasticized, filled-cell mixed-composite thermosetting plastic biopolymer. The word “polymer” denotes long-chain macromolecules which are crosslinked, such as proteins or starches. The word “plasticizer” indicates that water is the filling solvent that hydrates the polymer and supports its “plastic” behaviour.” (Review of comminuted and cooked meat product properties from a sol, gel and polymer viewpoint)
The optimal binding of water has been shown to be a balance between the creation of various base emulsions (for example fat and skin emulsions) and the inherent requirement for water as the plasticizer. In other words, there is a certain amount of water required to form the gel which is the basis of the product – all other water is better pre-bound. Adding “fillers” with high water-holding capacity such as soy isolate or TVP serves an important function of making the sausage less “rubbery”. LaBudde (1992) states it as follows. “Fillers with high water-holding capacity will effectively de-plasticize the system, resulting in lower strains to failure and higher stresses.” (Review of comminuted and cooked meat product properties from a sol, gel and polymer viewpoint). Like in whole muscle chemistry, we are looking at the role of bound, immobilized, and free water in the sausage matrix (see the section under “water” in Muscle Structure (Biology)
– Losing Some of the Water
Managing the process of water loss is of the utmost importance. Water act as the plasticizer in the system. In a frankfurter style sausage, “the proteins are gelled not only through the heat of cooking, but also through the mechanisms of water loss (shrinkage), pH (acid rinse) and smoke application.”
That water loss must take place and is important. “The effect of moisture loss through shrinkage is twofold: a drop in the plasticizer percentage and an increase in the percentage of other materials, including protein. Consequently, the strength of a “shrunk” product will be larger than that of the “unshrunk” product by at least the percentage shrink [ 1/(1-s) ], and the strain to failure lower by approximately the shrink [ 1-s ].” (Review of comminuted and cooked meat product properties from a sol, gel and polymer viewpoint)
Water loss is important but too much water loss is uneconomical. In the right drying, smoking and cooking chamber, the method of applying heat to the sausages, the rate of temperature application, humidity and wind speed (velocity) are key factors to control. From a business perspective, the role of an excellent personal banker is key to success. In terms of meat processing, the right smokehouse partner is as important as a personal banker to the overall business. They must be entrusted with the management of water or fat loss during the final cooking step. They are also the custodians of the final look of the product before packaging. Texture and gel formation is within their scope of responsibility. I cannot over emphasis the importance of choosing the right smokehouse and the right smokehouse supplier.
In producing these sausages, a customary South African formulation will result in between 15% and 18% moisture loss during the cooking cycle to 71o C. Kerres smokehouses technology promises a 30% reduction in this loss to between 10 and 13%. Trails are underway in Germany, using South African recipes, to confirm these. The overall loss we are targeting by using the correct product ingredients, along with the Kerres smokehouse technology I set at between 8% and 10%. These targets are ambitious, and results will be made available in updates of this article.
Old School Smoking/ Drying -> Latest Technology
“Kerres smokehouses technology promises a 30% reduction in smoking/ cooking loss”
Blending and Filling
The grinder -> mixer -> emulsifier -> filler configuration is retained with key adjustments in the state of the ingredients added at the various stages. The entire discussion of the mix of traditional processing technology using micro cutters and grinders and incorporating DCD’ed raw materials discussed above feature prominently under this heading. For Africa, I advocate the incorporation of Ethyl Lauroyl Arginate (LAE) in the product as one of the micro hurdles.
There is a trend in the rest of Africa (excluding South Africa) not to dry the sausages before sale and to use liquid smoke in the product composition instead of natural smoke. This is an unacceptable compromise because it seriously compromises the product quality, and our goal is to deliver more nutritious food to Africa of a quality equal to or higher than what is found in European and North American supermarkets in Frankfurter sausages.
I have found the Kerres team to be the best to outsource the final look, feel and texture of the product to. I base this statement on the versatility of their equipment. It is a familiar frustration to all production managers that they buy equipment and lock themselves into a certain processing system which invariably comes to haunt them later when they want to change the production system. In smokehouse technology, it is clearly seen in the choice between a system with vertical or horizontal airflow.
As a case in point, consider the change from natural or artificial casings and the emergence of alginate casing technology. The use of alginate casing technology has become widely available, in South Africa, through the spice supplier Freddy Hirsch, but when drying, the sausages can’t hang and are packed on trays which favours a horizontal airflow and not the vertical airflow systems used when smoking sausages that hang on smoke sticks and are linked together. So, ineffective smokehouses now become an obstacle when the production manager wants to change how the sausages are produced.
Even more, what do you do if you only want to change part of the processing system to alginate casings and still offer the consumers the natural or collagen casings they are used to?
The same applies to bacon processing technology. The traditional way is to hang the bacon in the smoke chamber. However, the latest method of bacon processing using grids to “shape” the bacon, favours again a horizontal airflow system as opposed to the vertical flow systems. The latter is favoured by the traditional way of hanging the bacon. (Best Bacon and Rib System on Earth)
Because drying/ cooking/ smoking is so important in the final product, it is surprising that many owners/ investors or managers base their decision on “an easy deal” or the cheapest option available to them. The wrong smokehouse partners are one of the most expensive mistakes we’ve made at Woody’s!
The Kerres smoker has a hybrid system that incorporates both horizontal and vertical airflow. They offer it as an added option, but in my mind, it is an easy decision!
Drying and smoking are dependent on many factors. Airflow is amongst the most prominent features. Below is a clip showing the Kerres system. The hybrid system is a stroke of genius. This system along with an introduction to the smokehouses of Kerres is dealt with in the video clip below.
Demonstrating the effectiveness of the hybrid smoking system
Below is a clip from a client of Kerres in the USA. Whether alginate casings are used for sausage production, or the grid system in bacon processing, the hybrid system is the best solution I ever came across. The clip below which I got from their website is absolutely astounding! See how close the shelves are stacked and how full they are loaded and have a look at the consistency! It is without a doubt the single most impressive display of what can be achieved in a smokehouse than I have ever seen!
Vegetable sausages are nothing new to areas in the middle east, but the West has suddenly woken up to this important product class when it realised its heavy reliance on meat-based diets presents health challenges that cannot be overcome apart from reducing the consumption of meat.
This area of application represents a feature of DCD Technology that cannot be achieved more effectively in any other way. Let me state it like this. DCD technology makes the high throughput production line of such sausages possible. It speaks to the essence of the approach I followed in re-evaluating the production of hybrid sausages two years ago (Nose-to-Tail and Root-to-Tip: Re-Thinking Emulsions).
The matter of final product packaging and shelf life is closely related as is shelf life and raw materials used in the blending and filling stage. In general, shelf life will be achieved through:
Level of water binding achieved;
Pressure from the DCD processing system of Green Cell on key ingredients;
The use of LAE both included into the meat mix as well as fogging the roll stock pouch after forming and fogging into the pouch after packing.
If applied correctly, this natural preservative will extend the product shelf life dramatically. The key to the effectiveness of the product is dosage and application method which we are in the process of addressing. Watch this space for updates and announcements!
Using the combined approach as outlined above yields unsurpassed shelf-life results.
Over the years I have seen the tremendous benefit in stepping periodically back from one’s work and re-evaluating everything I have learned and asking the question if there is not a better way of doing it. This is true when it comes to bacon production technology (Best Bacon and Rib System on Earth). I have not yet integrated a new application of the Kerres smoker technology to the article I just cited on bacon production, but I will do this over the weeks following and publish it as new and updated articles.
In our current consideration of the best Frankfurter style sausage system available, the Kerres smokehouse technology, along with LAE and DCD Technology draws years of work together into a complete and extremely versatile and productive system.
Africa is emerging as the future economic powerhouse and the driver of world markets, and I am honoured to be a small part of this awakening when it comes to meat processing technology.
Dr RA LaBudde does a great treatment of fine emulsions. There are of course many other excellent works on the subject but the language LaBudde used, I can understand!
I give the work of Dr LaBudde on the subject here in its entirety. It is important to remember that this is only one half of the equation. Meat processing is an art as much as it is a science. For the “art” we will feature the work of the Master Butcher from Saint Petersburg, from Russia, who gave the world fine meat emulsions, Petr Pakhomov.
The fact that we call the most famous fine emulsion sausage in South Africa, a Russian, comes from its Russian origin and was either introduced to South Africa by early immigrants or, more likely, by Russian volunteer who fought on the side of the Boers in the Anglo Boer War. Not just the Russians, but the people from the Balkans and Eastern Europe specialised in this and it was the Russians and East Europeans who brought this technology to America following World War One. People from the Russian steppe and surrounding regions pioneered the use of meat extenders and emulsifiers and fillers which probably developed from their milennia old soup technology. Fine emulsion sausages became important in America, after the war during sivere meat shortages. In central Africa the same sausage sold in South Africa as a Russian is called an Hungarian after the people who brough them the technology and traded it across the region. They produce it minus the showpieces and omitting these may be a later adaptation.
Petr Pakhomov is not just a Master Butcher, he is an artist and one of the best exponents of the art of fine meat emulsion. In a 2020 book he published on the subject, he writes: “This publication includes recipes for sausages from offal – an undervalued and rarely used raw material by sausages. On the counters of butcher shops there are hearts, liver, tongues – only these offal are well known to the townspeople and are in demand with them. The rumen, kidneys, brains, lungs, udders, properly prepared and cooked, are sometimes a discovery for people far from rural life. By-products allow you to create unusual in texture, very tasty, with a beautiful pattern on the cut, brawn, jellied, pate. A readily available and easy-to-use raw material is poultry meat. It serves as an excellent base for sausages and sausages, allowing you to play with taste thanks to the addition of various spice mixtures. The pale pink minced meat is a great backdrop for unusual cut patterns.”
“Of course, I have not ignored pork and beef products. My credo can be expressed by the words: “I paint with meat!” To make the sausage original, standing out on the counter among the usual – this task fascinates me. The appearance of the sausage product, the drawing on the cut should catch the eye of the buyer. Then comes the turn of consistency and taste, a successful combination of textures and spices.”
In this Petr strikes every single cord close to my hear and so, in celebration of his art and the science of Dr LaBudde I feature Petr’s work throughout the work of Dr LaBudde.
Comminuted and cooked meat products are viewed as water-plasticized, filled cell mixed-composite thermosetting plastic bio-polymer. This theoretical model is used to explain many factors influencing finished product quality attributes and to conjecture possible interactions between materials used in formulation. The relation between product texture and “bind” and “gel-strength” is described.
Meat Process Control Concepts
Meat Product Non-Chemical Properties
Meat as a Polymer System
Testing General Polymer Strength
Testing Meat Product Gel Strength Properties
Effects of Materials and Processing on Gel Strength
Skin vs Bulk Strength
Sensory Properties Influenced by Gel Strength
Typical Lot-to-Lot Variation in a Frankfurter’s Texture
Exhibit 1: Process Control Logic Exhibit 2: Force-Deformation Curve for Brittle Plastics Exhibit 3: Force-Deformation Curve for Ductile Rubbers Exhibit 4: Stress-Strain Relationship for Meats Exhibit 5: Typical Lot-to-Lot Variation in Stress for a Frank
Appendix 1: Glossary Appendix 2: Bibliography
Comminuted meat products include a wide range of consumable sausages: frankfurters, bologna, luncheon meats, smoked sausage, bratwursts, fresh sausage, ground meat, dry sausages and many others. We shall be principally concerned with cooked sausage which is intended to be bound together with some degree of strength in its manufacture. This is not intended to mean that this discussion is limited in applicability to these types of products, or even meat products in general, but to provide an example set of products for which the concepts described provide critical insight.
Most of the time we will be even more specific: the most frequent product examples used will be a frankfurter (cooked, fine-cut, eaten hot), a bologna (cooked, fine-cut, eaten cold) and a smoked sausage (cooked, ground, eaten hot). These particular products are sensitive to consumer perception of texture, represent a large volume of North American production and exemplify broad ranges of product categories.
Cooked sausage production of the frankfurter, bologna or smoked sausage types occurs in the following sequence of typical steps:
The raw meats to be used are first ground to medium fineness. For lean meats (< 30% fat) this means to 3/16″ (5 mm) and for fat meats (> 30% fat) to 3/8″ (10 mm) or larger.
The bulk of the meats used, together with 15% water and 2.5% salt and possibly sodium nitrite, are mixed together for 5 to 15 minutes at slow speed and dumped into vats.
The “preblended” meats of Step 2 are left to age for 8 to 24 hours.
A “final blend” is performed by mixing the “preblend” plus additional water together with sweeteners, spices and flavorings for 3 to 5 minutes.
The “final blend” is dumped into an emulsification mill(s) or a fine grinder (< 1/8″ or 3mm).
The fine-cut meat batter is stuffed into casings.
The stuffed product is showered with liquid smoke and 2 – 4 % acetic acid.
The product is cooked in a humidity and temperature controlled oven. A typical cook schedule might be: 30 min. @ 130 F (54 C), 30 min. @ 190 F (88 C). The humidity is low in the first stage, allowing the product to “shrink” and form a “skin”. The second stage will have a controlled humidity of at least 40% to promote rapid heat transfer. The product center temperature will be 160 to 170 F (71 to 77 C) leaving the oven.
The cooked product is showered with cold water or brine for 15 to 30 minutes to bring its temperature to 35 F (2 C).
The casings, if inedible, are removed by slitting and peeling.
The product is packaged under vacuum or modified atmosphere. Cooked meat products are composed of a variety of basic substances: moisture, fat and protein (comprising some 94% of the weight), salts (2 – 3%) and carbohydrates (3 – 4%). The carbohydrates include starches, sugars and fiber. These constituents are the real raw materials used in making meat products: the raw meats are simply variable “preblends” of moisture, fat, protein, etc.
2.0 MEAT PROCESS CONTROL CONCEPTS
Process control is composed of five basic steps (see Exhibit 1): 1) Measurement, 2) Standards or Targets, 3) Comparison of Measured to Standards, 4) Plan of Action, and 5) Implementation of the Indicated Action.
Obviously no control will be exerted if no observations of the process output are made (“open loop”). Similarly, measurements by themselves would supply little value if there were not a desired target to compare to, and if this comparison is not made, the size, if any, of the correction needed would be indeterminate. A pre-defined plan of action is essential to avoid “human-in-the-loop” over- and under-correction. The selection of which, if any, corrective action is needed must be based on the objective size of the difference from targets or standards.
It is very important to realize that proper control requires not only the measurements of the process average and its deviation from target, but also the process variation and its deviation from its standard operating range. Only after the process variation is brought under control is the process average a meaningful quantity.
Process control on cooked sausage involves measurement of average values and variation on basic analytical, nutritional, microbiological and sensory properties.
Generally by government regulation or company-imposed standards, the moisture, fat, protein, salt and nutritional content (calories, type of fat, cholesterol, vitamins, minerals and carbohydrates) and microbiological content of the product will be constrained to at least onesided limits.
Process planning and control on such analytical attributes is based on the following typical steps:
Each raw material used (meats, flavorings, etc.) is characterized by laboratory analysis of successive lot samples. The frequency of sampling and accuracy of analysis is tailored to be sufficiently predictive without excess expense.
Each product batch is formulated to obtain a desired target value on each attribute. The target is designed to provide protection against process and material variability causing the actual production lot value from violating the outgoing specification requirement.
For easily measured attributes (moisture, fat, protein), a laboratory analysis of the production blend may be performed, and the error in target reduced by addition of “correction” materials in the final blend.
Samples of production lots are taken as packaged and subjected to quality assurance testing to verify compliance with outgoing specifications.
In addition to analyte attribute control, consumer acceptance of a product requires sufficient consistency in certain sensory properties of the cooked sausage. The attributes of most importance include:
Bulk Texture or “Bind”
Flavor (from spice, etc.)
Shrinkage (Moisture loss in processing)
With the exception of net weight, these attributes are subject to only internally-imposed limits. Consequently the means of their control require development of methods not required or sponsored by regulatory organizations. The development of methods of measurement and control has therefore been left to company or university research and has lagged behind the other attributes non-specific to meat products.
3.0 MEAT PRODUCT NON-ANALYTICAL PROPERTIES
The cooked sausage non-analytical properties mentioned above (texture, color, etc.), although not determinable by chemical analysis, are still important to monitor and control.
Skin texture is the chief component of the “bite” of a product. The skin is “tougher” than the product interior provides an initial “snap” during eating. Products with edible (natural or collagen) casings can be manufactured as tough as desired. Skinless products only retain a softer protein-based skin due to smoke, acid and initial oven treatments. A proper balance between skin and internal texture is necessary. Too tough a skin will create the sensation of a “mushy” interior, which may be squeezed out of the skin during biting. Too soft a skin will cause the product to be uniform in texture with little “snap”.
Skin color is principally determined by smoke and acid treatments, and secondarily by the initial oven stage (temperature and humidity) and meat pigment content. Skin color is of importance only in small diameter product, and its darkness is a matter of taste. In products where skin color is important, consistency from batch-to-batch and within-batch is the primary issue.
Bulk texture is the chief component of the “chew” or intermediate and final texture on eating. Too weak a bulk texture and the product will seem “mushy”, too tough and the product will seem “rubbery”. Bulk texture is of critical importance in sliced product, or product with special strength needs, such as corn dogs.
Similarly, bulk color is of importance only in sliced products. Bulk color is determined almost entirely by nitrite level, meat pigment content and the final cook stage time and temperature. Preblend holding time is also a factor.
Saltiness, sweetness and flavor are normally controlled by set addition levels of salt, sweeteners and flavorings in the blend. No measurement normally occurs, with the exception of routine taste tests.
Purge loss or “syneresis” is a serious issue in vacuum packaged products. Significant liquid in the package creates the impression of defective or spoiled product. This liquid is an inconvenience to the consumer (drainage from package after opening) and encourages bacterial growth. Purge loss in bulk-packaged products may cause container damage or contamination, and will affect the net weight per unit of the product at the time of use.
Net weight per package or per unit is a function of stuffing level, process shrink and purge loss. Variation in stuffing level or cook shrink will cause variation in the net weight at the time of packaging. Excessive net weight variation will directly increase product weight “giveaway”. Product used in further processing, such as “corn dogs”, may have problems meeting its final combined product labeling requirements.
4.0 MEAT AS A POLYMER SYSTEM
Meat products have long been subject to mis-classification by researchers using inappropriate technical terms.
In the 1960’s and 1970’s the uncooked meat batter was described as an “emulsion” and the “emulsifying” properties of the meat proteins were thought to dominate the development of cooked product textural attributes. This led to flawed arguments regarding causal relationships between processing, materials used and final product properties.
From the late 1980’s to the 1990’s, researchers discarded the “emulsion” concept for a different viewpoint of a meat “sol” converting to a “gel” upon cooking. These terms are, however, still misnomers since “sol” and “gel” are applicable only to dilute (< 10%) colloidal dispersions.
Technically the uncooked meat mixture is a “paste”, not an “emulsion” or “sol”, since solids content is 40% or more. Upon cooking to a high enough temperature, the “paste” sets to hardened “plastic” material.
Because of these misclassifications, there is considerable confusion in the use of colloid science terms to describe meat systems. To avoid creating an entirely new vocabulary, we will use the current terminology of “gelling” or “gelation” synonymously for “setting” or “hardening”.
“Meat” is the protein-rich flesh of animals. For our purposes here, fish and poultry flesh are “meat”. As stated before, cooked sausage products are a mix of water, fat, protein, salts and carbohydrates gelled and set into a solid mass by the application of heat.
The principal functionality in forming the gelled and set mass comes from the long-chain proteins present and to a lesser extent from the long-chain carbohydrates (starches and gums). When the meat paste is heated above the set-point temperature, the long-chain molecules, supported in solution or at least hydrated by water, are forced to partially uncoil and form irreversiblez cross-linkages. The result is a three-dimensional crosslinked matrix which incorporates the water, fats, salts and fillers within its structure.
A simple paradigm for the mechanism involved is the hard-boiling of a common hen’s egg. The egg is initially liquid and is composed mostly of protein and water with a small amount of fat. When heat is applied above the “set-point” temperature, the protein unfolds and aggregates, forming the rubbery hard-boiled egg consistency. As is obvious, the water component is just as essential as the protein component: dried eggs do not hard boil! The water hydrates the protein molecules and allows mobility for unfolding and crosslinking.
The salts present in the water phase help ionically stabilize the unfolded protein molecules so that its structure can be more easily exposed. The function of salt may be easily seen by adding it to the water used to hard-boil an egg. If the shell is cracked so that a streamer of egg-white is forced out by internal pressure on heating, the presence of salt in the water will cause it to instantly coagulate and seal the crack.
To some extent fats also stabilize hydrophobic protein exposure. They also serve, with other water-insoluble components, simply to fill space and stiffen the protein matrix formed.
Starches and gums will hydrogen-bond and crosslink similar to proteins, and bind appreciable amounts of water. Generally the gelling temperature for such compounds is 90 C or higher, which is seldom obtained in meat processing. Non-gelling or insoluble carbohydrates principally act as mild water binders and matrix fillers. The strength of water-binding is moderate and due to capillary action and hydrogen-bonding, as opposed to irreversible crosslinking. The crystalline nature of a cooled starch gel results in a brittle texture which has little strength after fracture.
Non-meat proteins which are soy- or milk-based (soy flour, soy protein concentrate, soy protein isolate, whey protein concentrate, whey protein isolate, casein) have gel-points of 90 C or more, and function similar to starches in hydrogen-bonding with water to form weak gels at low temperatures.
Since meat’s texture is due to its property of heat-induced long-chain gelling or setting, cooked meat is classifiable as a water-plasticized, filled-cell mixed-composite thermosetting plastic biopolymer.
The word “polymer” denotes long-chain macromolecules which are crosslinked, such as proteins or starches.
The word “plasticizer” indicates that water is the filling solvent that hydrates the polymer and supports its “plastic” behavior.
The word “mixed” denotes possible crosslinking between different polymers, such as different proteins or proteins and cross-linked gums or starches.
The “fillers” present in meat products are fat or insolubles: in rubber tires, it is the carbon that makes the rubber black. Fillers normally will “stiffen” a plastic or rubber, making it harder and less stretchable. Sometimes fillers are active (such as the carbon in rubber tires) and actually bind to the setting polymers present. In this case the filler may increase strength dramatically (ten times or more), and out of proportion to its relative presence on a formula basis.
Additional plasticizer will soften and make more stretchable the polymer matrix. Removal of plasticizer will make the plastic harder and more “brittle” (i.e., less stretchable).
Skin texture in casingless product is formed in a more complicated manner. The proteins are gelled not only through the heat of cooking, but also through the mechanisms of water loss (shrinkage), pH (acid rinse) and smoke application. Therefore only proteins and carbohydrates which gel under these conditions will reinforce “skin” formation. Other materials will in general weaken skin strength by dilution or formation of flaw points.
5.0 TESTING GENERAL POLYMER STRENGTH
In order to understand the significance of tests performed on meat products, it is necessary to first review the mechanical strength principles of the general polymer system.
There is an extensive literature associated with the theory and testing of the mechanical strength or plastics, rubbers and composites. (See Appendix 2.)
The terminology of mechanical properties is vague and confusing, since it has developed to describe the results of very specific test techniques. Appendix 1 gives a glossary of definitions of most common terms.
A typical experiment consists of applying a changing force needed to maintain a constant rate of deformation of a test specimen of specific shape (cross-section and length). The fraction deformation in the direction of force is called the “strain” and the force per unit cross-sectional area is called the “stress”. In experiments where theory is not easily applied, the force and deformation are reported. Where geometry can be analyzed properly, the stress and strain are reported. Force is usually measured in Newtons (N) or kilograms-force (kgf). Deformation is reported as % change. Stress has units of Pascals (usually megapascals, MPa). Strain is dimensionless.
Tests may be performed by compressing, stretching (tension) or twisting (torsion) the specimen. For brittle materials, different strengths are obtained for each mode of testing. For ductile materials, the results from different modes are close.
Measurements of stress and strain for very small deformations allow characterization of the elastic properties of a material, chiefly the Modulus of Elasticity (compression/tension) or Rigidity (torsion).
Large deformations (more than a few %) lead to plastic behavior where the material starts to yield under stress. In this case the quantities of interest are the Maximum Stress and Strain at Maximum Stress. Most tests do not strain the material to more than 25% of its original length, because of unusually behavior occurring when the geometry undergoes large changes.
Viscoelastic and viscoplastic materials are sensitive to the strain rates used in testing: fast rates require higher stresses. As a consequence tests are done at an accepted or specified strain rate, or must be repeated at various strain rates.
Testing done on general polymers falls into three categories:
ELASTIC TESTING: Done at low levels of deformation, usually by oscillatory stressing to determine dynamical properties of the modulus at various strain rates.
FAILURE TESTING: Done at large levels of deformation, usually at a constant strain rate, until the specimen breaks. The reported values are Break Stress and Break Strain.
MODULUS TESTING: Done at fixed levels of strain, such as 90% or 75% (greater than 75% is not recommended). The stress required to achieve this level of deformation is reported.
The dynamical Elastic Testing is normally done only in research. Failure testing is done in research, where usually the whole stress-strain curve is reported, or as an engineering test to quantify the strength at failure. Modulus testing is routinely used in quality control on polymers with important mechanical properties.
Exhibit 2 shows a typical stress-strain curve for a brittle material, such as concrete or styrofoam. Note that at a particular level of strain the material fractures suddenly and the stress required drops to zero.
Exhibit 3 shows a typical stress-strain curve for a ductile or rubbery material, such as polyurethane. Note that after a certain stress or strain occurs, the material starts to yield (become plastic) and the stress drops and appears to fail to a nearly constant value while the material creeps. Once a certain strain occurs, the material becomes harder again (all the “give” used up) and the stress increases to another maximum before the material breaks.
In both Exhibits 2 and 3 you will notice that the initial portions of the stress-strain curves are straight lines (with a slope of the Modulus): this is the Proportional Region. Before the material starts to yield in Exhibit 3, the material would return to nearly its original shape if the stress were removed: this is the Elastic Region. In the testing of rubber-like materials, it is not infrequent to find an absence of the linear Elastic Region. These materials “strain-harden” continuously to a new material whose Elastic Region is approached after noticeable elongation.
In order to specify the mechanical properties of a general plastic, it is usually sufficient to report the Modulus of Elasticity (compression), Modulus of Elasticity (tension), Modulus of Rigidity (shear) and Maximum Stress and Strain for each mode.
6.0 TESTING MEAT PRODUCT GEL-PROPERTIES
The importance of texture has led to a variety of measurement methods in the last three decades. They fall into the raw material and outgoing product test categories.
6.1 SAFFLE “BIND” TEST ON MEATS
The dominant effect of meat salt-soluble proteins on the resulting texture of the product led in the 1960’s and 1970’s to the “Georgia Bind” test of Saffle and co-workers (see Appendix 2 for references).
This test involves the extraction of salt-soluble protein from raw meat samples in a standard way, and then determination of a relative functionality of this salt-soluble protein by an oilemulsification test. The amount of oil sustained in a blender at a particular speed for a particular (10 mg/ml) concentration of salt-soluble protein defines the functionality of that protein. Combining the two effects of % protein salt-solubility and oil-functionality gives the “Bind Constant” or “Bind Index” for the meat.
The “Bind Constants” determined are then used to formulate a product to a specified level of texture, usually specified as the average of
Bind Constant x Protein x 100 %
on a finished weight basis. The resulting “BIND” levels formulated to are typically 200 – 220 % FW for beef products, 180 – 190 for 30% beef and 30% pork products, and 170 – 180 for pork dominant products. Poultry products vary from limits set to 170 – 180 (similar to pork) for products formulated to tighter specifications, to 250+ for chicken franks that are low fat and not adjusted to maximum water content.
The “BIND” values for raw meats are seldom actually measured. Instead, the tabulated results of the Saffle workers are used, possibly adjusted for proximate analysis variations (via the QC Assistanttm of Least Cost Formulations). The presumption is that the “Bind Constants” for the actual meat lots are not too far from the tabulated values, particularly when adjusted for proximate analysis differences.
This “BIND” concept has worked fairly well in practice over the last two decades. Change of the formulated “BIND” of 10 to 15 units will usually result in a sensible change in texture. The standard deviation of measurement of the original “Bind Constants” was approximately 5 to 7%, about the same as the 10 to 15 units is to the 170 to 220 unit limit.
The principal difficulties with the “BIND” concept are:
The concept is inapplicable to many fillers and binders.
The test is not easily repeatable between laboratories because the methodology is sensitive to equipment used.
The effects of processing are not considered and assumed constant.
The effects of fat and moisture are not determinable, other than of dilution, and modern meat products have shifted from 30% fat to 10% fat and lower.
The Saffle “BIND” concept has, whatever its limits, revolutionized meat product formulation accuracy and has provided a basic solution to texture control in cooked sausage.
6.2 OUTGOING PRODUCT COMPRESSION TESTING
The few large meat companies which can afford pilot plants in their R & D facilities will usually also include a Universal Tester system (such as Instron, Chatillon or others).
These testers can perform vertical compression or tension tests at constant strain rates in a heavyduty test stand with a chuck to contain a test probe and a force gauge (of at least 1% full-scale accuracy) to measure the stress applied. The tester provide chart recorder output which indicates force vs time (which gives deformation via the constant strain rate) for the entire crosshead movement.
Because of the design of the machine and the properties of the meat samples being tested, usually a compression test is performed using either a cylindrical, flat probe of 5 to 12.5 mm diameter, or a spherical probe of 5 to 10 mm diameter. The spherical probe test with a 10 mm ball is routinely performed on all lots of surimi.
Universal Testing Machines cost from $5,000 to $20,000 or more, depending on features.
The most reliable compressive test is measurement of the peak force required to puncture the sample. As deformation occurs, the stress rises rapidly and linearly to a first maximum, then undergoes a complex pattern, followed by a second maximum and then failure. Unfortunately there is little consensus as to the shape of the probe (flat vs ball) or which point on the force vs deformation curve to use as the measurement. Some investigators report the first maximum, others the second. It appears that only the first maximum is a reliable predictor of the material properties, since the curve after initial puncture is subject to side friction. In addition, the test results are influenced by the rate of cross-head speed and the diameter of the probe used, all of which vary between investigators.
Other labs report the results of compression to a fixed deformation, such as 90% of height, 80% of height or 75% of height and sometimes even 50%. These tests are particularly difficult to reproduce, since these fixed deformations are not extrema in the force vs deformation curves but instead are on a side slope of rapid change. Consequently slight changes in mounting, deformation or material or cross-head speed may result in significantly different forces being measured.
In the best of circumstances, the precision of the measurement between replicates is 5 to 10%, chiefly due to the incomplete homogeneity of the meat product structure (4 to 6%) and its response to the compressive deformation. Tests are usually run on 5 to 10 replicates to average out within product and instrument variation.
Only the surimi industry has standardized the probe and cross-head speed for the compression test to failure: a 10 mm diameter spherical ball. No standard of any time seems to exist for this type of test in the meat industry.
Because of the inability to apply theory to the complex deformations and unknown contact surfaces involved in the vertical compression test, the results are normally reported as force and deformation rather than stress and strain. A nominal stress of doubtful validity could be obtained by dividing the flat and spherical probe forces by p r2.
6.3 OUTGOING PRODUCT TORSIONAL TESTING
A recent and increasingly popular method of meat product texture measurement is the torsional “gelometer” developed by Lanier and Hamann at North Carolina State University (see Appendix 2 for references).
This system twists a standard hourglass-shaped specimen at a constant angular rate (2.5 rpm = 15 degrees/s) until it fails. The entire stress-strain curve is available, with the maximum stress and strain reported.
The specimen is cut to a standard length (about 20 mm) and plastic plates are glued to each end.
The standard hourglass shape is obtained by chipping a specimen to shape using a special knifetoothed lathe wheel. The sample is necked to 10 mm + 0.2 mm.
The specimen in mounted in a specially modified Brookfield viscometer with a 1% full-scale accuracy digital head. The specimen is rotated by turning the top plastic plate while the bottom plate is held fixed.
This test is relatively well-designed, with the geometry of the specimen chosen to be amenable to theoretical analysis. The force and rotational deformation are easily converted to nominal stress and true strain by the application of formulas incorporating the specimen geometry, rotational speed and effect of twisting.
The stress and strain measured in the NCSU torsional gelometer are statistically independent measurables. The reproducibility of strain is about 4 to 6% standard deviation, and of stress about 5 to 10%. The stress error is inflated by the 5% typical instrument error at the 20% of fullscale encountered on meat products. From 5 to 20 replicates are usually run to average out between specimen and instrument errors.
Because of its sound theoretical basis, the NCSU gelometer is the instrument of choice for research, providing a detailed stress-strain curve for each test. It is, however, much more laborintensive than other test methods, due to milling of the specimen.
The NCSU torsional gelometer is available at a cost of about $15,000 from Drs. Lanier and Hamann (Gel Technology, Raleigh, NC).
7.0 EFFECTS OF MATERIALS AND PROCESSING ON GEL-STRENGTH
Cooked meat products, such as frankfurters or bologna, are, as mentioned before, filled cellular plastics where a three-dimensional cross-linked protein structure encapsulates water, fat and fillers.
Time of chopping or mastication will affect final strength, due to development of active ends of severed protein molecules. In addition chopping reduces fat particle size, breaks the containing fat cell layers, and melts fat droplets allowing surface smearing to take place.
Because meat products are composed of protein macromolecules which retain some alignment of the direction of stuffing, they exhibit “anisotropy” or directionality of strength. The stress and strain to failure will in general differ longitudinally and laterally to the stuffing axis. The effect of stuffing is to pre-stress and pre-strain the product in the direction of stuffing, reducing the longitudinal strain possible and stiffening the gel.
As a product ages in the package after production, it will gradually relax the embedded strain which has been “cooked” into the gel, increasing the strain and decreasing the stress needed for failure.
Filled composites generally exhibit increased strength in compression and decreased strength in tension. Consequently it would generally be expected that adding inert or insoluble materials (and displacing moisture) will stiffen the structure to compression and lower the strain needed for failure. However both stress and strain would be lowered in tension.
As a consequence, adding such fillers not bound to the stronger protein structure would be expected to lower skin strength, where the test condition is perpendicular to the skin, resulting in failure by shear or tension. Such fillers include non-gelling proteins, fats and carbohydrates.
Since moisture functions as a plasticizer, increasing moisture content would imply increased ability to strain, and a softer product (due to displacement of non-liquid ingredients).
Strength and strain at failure will be directly related to protein content: under ideal circumstances proportional to the active protein.
The effect of moisture loss through shrinkage is twofold: a drop in the plasticizer percentage and an increase in the percentage of other materials, including protein. Consequently the strength of a “shrunk” product will be larger than that of the “unshrunk” product by at least the percentage shrink [ 1/(1-s) ], and the strain to failure lower by approximately the shrink [ 1-s ].
Fillers with high water-holding capacity will effectively de-plasticize the system, resulting in ower strains to failure and higher stresses.
The time and temperature the product is cooked at will have a modest influence on the gel strength. Product cooked to 5 C or 10 C higher temperature or for 10 minutes longer will generally gel more fully, resulting in both increased stress and strain at failure. Since the gel process is analogous to the microbiological “kill” effect of cooking (bacteria are proteins too!), it is easy to see that cooking has a natural completion, where nearly 100% conversion occurs. Therefore very short cook cycles the lowest final temperatures will exhibit the greatest sensitivity to these variables.
The effects of salt level are to shift the pH sensitivity of the proteins and stabilize functional groups to the surrounding water. Higher salt levels generally will increase strength due to greater protein mechanical extraction, greater unfolding (resulting in increased cross-linkages) and lower the gel point temperature (resulting in more complete gelling in the cook cycle).
The effects of phosphate or lactate include:
1) increase in ionic strength (salt effect),
2) increase in pH and
3) special interactions to stabilize unfolded proteins.
Skin formation is generally due only to the meat myofibrillar proteins. The higher shrink losses from the skin areas mean the structure is pre-strained and stressed. Displacement of the moisture plasticizer by any non-bonding materials will generally decrease the strain to failure, making the skin more brittle. Since the skin properties of interest are normally tensile or shear strengths, such fillers will generally also decrease the skin strength, or at best leave it unchanged.
The mechanism for meat product deformation of 100% to 150% before failure is due to the protein chain length. The long protein molecules may be visualized as springy coils which are crosslinked to neighboring coils in random patterns. When strain occurs in a specific direction, the protein molecules uncoil into a more linear conformation. This requires free space (solvated by plasticizer) and mobility to accomplish. Clearly there is only so much “uncoiling” that can occur: if pre-stretching is accomplished by volume compression due to cook shrink or by stuffing distortion, less deformation will be available during testing or eating.
The protein content of cooked meat products is usually between 10 and 20% of the composition, or a minor constituent compared to moisture and fat. Consequently the stress and strain observed for a product will increase at least linearly with protein, and quadratically for low levels of protein.
Collagen protein contracts by 10% or more upon reaching its gel-point of 60 C, and therefore has the effect of straining the entire thermoset product.
Fat generally expands by 10% or more upon melting, and therefore stresses and strains the product before complete setting has taken place. It is essential that the fat droplets be coated with a closed-cell protein structure or embedded in a strainable gel to protect the structure against fracture by fat expansion with concomitant leakage of liquid fat along these fractures to relieve the stress imposed.
It is an interesting fact that most cooked muscle foods exhibit a modulus of rigidity between 10 and 20 kPa (see Exhibit 4).
The ultimate stress needed for a particular product will change substantially with the temperature at time of test. The viscosity of the fat present will change markedly below room temperature as the fat congeals and becomes crystalline. The stress needed at 35 F may be twice that at 70 F. The ultimate stress above room temperature should drop at least linearly with increasing temperature up to the gel-point at a rate of 0.1 – 0.3% per degree C.
8.0 SKIN VS BULK STRENGTH
As mentioned in the last sections, there is a fundamental difference in the mechanical properties of interest of the skin and of the bulk product:
PROCESSING: Skin properties are primarily and directly affected by processing steps such as smoke treatment, acid treatment and early cook stages. Bulk properties are, however, primarily affected only by the final cook stage.
TENSION vs COMPRESSION: The skin is bitten through perpendicular to its surface, so strength in tension and shear are the quantities of interest. The bulk interior is masticated by chewing, which means that strength in compression and shear are the quantities of interest.
FILLERS: Fillers, such as fats, carbohydrates, non-meat proteins, etc., generally will decrease skin strength, even though the meat protein level stays the same, but will generally increase the bulk strength, even if the moisture level is unchanged.
MECHANICAL SUPPORT: Testing of specimens for skin strength involve imposition of perpendicular loads to a thin layer, drawing upon mechanical support from the product surface large distances away. On the other hand, bulk compression or shearing remains local, so long as the test probe used is small in invasive volume. As a consequence, independent measures of skin strength and bulk strength should be made.
9.0 SENSORY FACTORS INFLUENCED BY GEL STRENGTH
The “+” in the above table indicates the parameter is positively highly correlated with the factor (e.g., increasing maximum stress increases hardness). A “-” indicates the parameter is negatively correlated with the factor (e.g., increasing maximum stress lowers ease-of-swallow). No entry in the table indicates no significant direct correlation.
As mentioned before, skin and bulk texture need to be considered separately. A “good” frank, for example, should have enough skin strength to provide a noticeable “snap”, but not so strong that it is difficult to bite or so that the frank “bursts” on eating. The bulk texture should be strong enough to be “chewy”, but not so strong as to appear “rubbery”. Some markets (e.g., Far East) or some products (e.g., canned Vienna sausage) may require a “mushier” product standard than North American franks.
10.0 TYPICAL LOT-TO-LOT VARIATION IN A FRANKFURTER’S TEXTURE
Exhibit 5 shows an actual record the ultimate stress (as determined by the NCSU torsional gelometer) of successive batches of a frankfurter over days of production.
EXHIBIT 1: PROCESS CONTROL LOGIC
EXHIBIT 2: FORCE-DEFORMATION CURVES FOR BRITTLE PLASTICS
EXHIBIT 3: FORCE-DEFORMATION CURVES FOR DUCTILE RUBBERS
EXHIBIT 4: STRESS-STRAIN RELATIONSHIP FOR MEATS
EXHIBIT 5: TYPICAL LOT-TO-LOT VARIATION IN STRESS FOR A FRANK
APPENDIX 1: GLOSSARY
Binder: In a composite plastic, the continuous phase that holds together the reinforcing materials.
Break, Failure or Fracture Strength: The stress at the breakpoint.
Break, Fracture or Failure Point: The discontinuous point at which the specimen separates and the stress drops to zero rapidly.
Brittleness: The property of a material to fail under a small deformation.
Brittle materials usually behave differently under tension and compression.
Brittle materials are usually weak in tension and strong in compression.
Cell: A small cavity surrounded partially or completely by walls.
Cell, Open: A cell not totally enclosed by its walls.
Cell, Closed: A cell totally enclosed by its walls.
Colloid: A substance in an extremely fine state of subdivision dispersed in a continuous medium, where the principal properties of surfaces and interfaces play the dominant role.
Colloidal solution: A dilute colloidal dispersion of a lyophilic particles, usually molecularly dispersed and thermodynamically stable as a single-phase system.
Creep: The time change of strain under a fixed stress.
Crosslinking: The formation of a 3-dimensional polymer by means of interchain reactions resulting in changes to physical properties.
Deformation: The decrease in length from the gage length due to compressive force applied.
Dilatant: A material which hardens upon imposed shear. (Opposite of “Thixotropic”.)
Disperse phase: The discontinuous phase of a colloidal mixture.
Dispersion medium: The continuous phase of a colloidal mixture.
Ductility: The property of a material to have large plastic deformations without rupturing.
Ductile materials have almost identical tension and compression stress-strain curves.
Elasticity: The property of returning quickly and completely to initial geometry after unloading.
Elastic Limit: The greatest stress to which a material may be subjected without permanent strain resulting (i.e., the specimen recovers its original dimensions).
Elastomer: A macromolecular material that at room temperature returns rapidly to approximately its original dimensions and shape after a substantial deformation by a weak stress.
Elastoplasticity: The property of retaining partially and permanently a deformation after unloading.
Electrophoresis: The movement of particles with respect to a liquid as a result of an applied electric field.
Elongation or Extension: The increase in length from the gage length due to the force imposed.
Emulsion: A stable dispersion of one liquid in another, usually water and an oil or organic compound. Two types exists: oil-in-water (“O/W”) and water-in-oil (“W/O”), depending on which compound is the disperse and which is the continuum phase. Stability requires the presence of a third material, an “Emulsifying Agent”, which stabilizing the oil/water interface.
Fiber: A plastic which has been crystallized by “Strain Hardening” to form a greatly stronger oriented or interlocking structure longitudinally.
Filler: A sometimes inert and sometimes functional material added in the particulate solid phase to a plastic to modify its properties or lower its costs. If functional to a high degree, they are called “Reinforcing Fillers”.
Flexibility: The property of a material to have large elastic deformations without rupturing.
Foam: Gaseous dispersion (usually air) in a liquid continuum.
Gage Length: The original length of a test specimen over the portion over which the strain is being determined. For tensile or compressive tests, the height of the narrow region. For torsional tests, the circumference of the narrow region.
Gel: A two-component semi-solid system, rich in liquid (< 10% gelling component), made of a network of solid aggregates in which liquid is held. A hardened “sol”.
Gelation: The process of hardening or “setting” of a sol into a material with solid-like properties.
Gel-Point: The stage at which a liquid mass begins to exhibit pseudo-elastic behavior, the inflection point in viscosity vs time.
Glass: A product of freezing, typically hard and brittle, which has cooled to rigidity without crystallizing.
Glass Transition: The reversible change over a relatively small temperature region in amorphous polymers to a viscous or rubbery condition from a hard and brittle condition.
Glass Transition Temperature: The approximate midpoint of the temperature range over which a glass-to-rubber transition occurs. Hofmeister series: See “Lyotropic Series”.
Hydrocolloid: A material capable of forming a colloidal suspension in water.
Hydrogel: A gel formed from a material dispersed in water as a medium. Hydrophilic: A disperse phase which has a high chemical affinity for the water dispersion medium.
Hydrophobic: A disperse phase which has a low chemical affinity for the water dispersion medium.
Lyophilic: A disperse phase which has a high chemical affinity for the dispersion medium.
Lyophobic: A disperse phase which has a low chemical affinity for the dispersion medium.
Lyotropic series: A series of cations or anions in order of coagulating power (e.g., Li+ > Na+ > K+ or Cl- > Br- > I-).
Micelle: A submicroscopic aggregate of colloidal polymers usually oriented with respect to a dispersion medium (lyophilic out and lyophobic in).
Modulus of Elasticity or Elastic Modulus or Young’s Modulus: The slope of stress vs strain below the proportional limit in tensile or compressive testing.
Modulus of Rigidity: See Shear Modulus.
Necking: localized reduction in cross-section in tensile tests.
Nonrigid Plastic: A plastic which has a modulus of elasticity of 70 Megapascals or less. All cooked food gels have moduli of 1 MPa or less.
Pascal: A unit force of 1 Newton applied to a cross-sectional area of 1 square meter. 1 atmosphere of pressure is 101325 Pa or 101.325 kPa or 0.101325 MPa.
Peptization: From analogy to peptic digestion, the spontaneous dispersion of a precipitate to form a colloid.
Percentage Elongation: The elongation expressed as a percentage of gage length. Different percentage elongations will be observed at yield and at break.
Paste: A concentrated (> 10% by volume) dispersion of solid particles in a liquid continuum.
Plastic: A material that has as an essential ingredient one or more organic macromolecule, is solid in its finished state, and at some stage in processing can be shaped by flow. Rubbers, textiles, adhesives and paint are not classified as plastics.
Plasticity: The property of retaining permanently and completely a deformed shape after unloading.
Plasticizer: A substance incorporated in a material to increase its workability, flexibility or distensibility.
Plastisol: A plastic or resin dissolved in a plasticer to give a pourable liquid.
Polymer: A substance consisting of repeating units of one or more monomers.
Proportional Limit: The greatest stress for which stress vs strain is a straight line through the origin.
Purge: The syneresis of water from a meat product over time.
Rate of Straining: The change in nominal strain per unit time. Plastic materials become “stiffer” when faster deformations are required. Consequently results at different strain rates will generally differ significantly in a systematic manner. For non-rigid materials, usually 1.5 per minute (150% elongation in 1 minute or 2.5% per second).
Rate of Stressing: The change in nominal stress applied per unit time. See Rate of Straining.
Reinforced Plastic: A plastic with high-strength fillers embedded, resulting in mechanical properties enhanced over the unfilled plastic.
Rheology: The study of mechanical properties, particularly flow, ductility and plasticity, or concentrated colloidal systems.
Rubber: A material capable of recovering from large deformations quickly and forcibly. From a test point of view, a rubber will retract from 100% elongation to 50% elongation in less than 1 minute at room temperature.
Shear Modulus of Elasticity or Modulus of Rigidity: The slope of shear stress vs strain below the proportional limit in torsional testing.
Sol: The dilute (less than 1% by volume) dispersion of a lyophobic solid in a liquid or gaseous medium. The dispersion medium is usually denoted by a prefix, such as “hydrosol” (water) or “aerosol” (air).
Strain or Nominal Strain: The ratio of elongation or compressive deformation to gage length. If the specimen retains its original dimensions, the strain is 0. Note that, as with nominal stress, strain may not be meaningful if the specimen geometry is seriously distorted during test.
Strain Hardening: The process of increasing strength by elongation by strain to produce apartially crystallized fiber.
Strength, Nominal: The maximum nominal stress sustained by the specimen during the test.
Stress, Nominal: The force per unit area (N/m2 = Pascal) of minimum original cross-section. If the specimen deforms significantly under test (“yields”), necking, stretching or bulging may occur to an extent that the nominal “stress” is not a meaningful quantity.
Syneresis: The spontaneous shrinkage of a gel to form a more concentrated gel and free exuded dispersion medium.
Thermoplastic: A plastic that can be repeatedly softened and hardened by heating and cooling to and from a flow-shapable state.
Thermoset: A plastic that, after having been cured by heat or other means, is substantially infusible and insoluble.
Thixotropic: A material which has lowered viscosity on increased shear (e.g., liquefied by shaking). Notable example is quicksand, which acts liquid under force.
Toe Compensation: The correction for the initial “ramp-up” of stress required to take up equipment slack at the start of testing.
Toughness: The property of a material to withstand large deformations or stresses before failure.
True Strain: The strain corrected for known standard geometry changes necessary under test which affect length. For a tensile test, true strain is the natural logarithm of 1 plus the nominal strain (ratio of after to before length).
Ultimate Strength or Maximum Strength: The maximum stress encountered during testing.
Viscoelasticity: The property of continuously creeping under load and continuously retreating after unloading, with a return to original form after some lapse of time.
Viscoplasticity: The property of continuous creeping under load and a retention of the deformed shape after unloading.
Viscosity: The resistance to flow within the body of a material.
Work to Failure or Fracture: The integrated force through deformation or stress through strain to cause breakage or rupture of the specimen. A measure of “Toughness”.
Yield Point: The first point at which the strain increases without an increase in stress. Usually at a maximum in stress, but may also be at an inflection point in stress.
Yield Strength: The stress at the yield point.
APPENDIX 2: BIBLIOGRAPHY
Annual Book of ASTM Standards, Volume 8.01: Plastics, American Society for Testing and Materials, Philadelphia, PA.
Colloid Science, A.E. Alexander and P. Johnson, Oxford University Press, London, 1949.
Determination of Elastic and Mechanical Properties, B.W. Rossiter and R.C. Baetzold eds., Physical Methods of Chemistry VII, J. Wiley & Sons, New York, 1991.
Food Colloids, R.D. Bee et al. eds., Royal Society of Chemistry, 1989.
Food Emulsions, K. Larsson and S.E. Friberg eds., 2nd Edition, Marcel Dekker, New York, 1990.
Food Proteins, J.R. Whitaker and S.R. Tannenbaum, AVI, Westport, CT, 1977. Food Texture, H.R. Moskowitz ed., Marcel Dekker, New York, 1987.
Functionality and Protein Structure, A. Pour-El ed., ACS Symposium Series 92, American Chemical Society, 1979.
Hydrophobic Interactions in Food Systems, S. Nakai and E. Li-Chan, CRC Press, Boca Raton, FL, 1988.
Interactions of Food Proteins, N. Parris and R. Barford eds., ACS Symposium Series 454, American Chemical Society, 1991.
Microemulsions and Emulsions in Foods, M. El-Nokaly and D. Cornell eds., ACS Symposium Series 448, American Chemical Society, 1991.
Muscle as Food, P.J. Bechtel ed., Academic Press, New York, 1986.
The New Science of Strong Materials, J.E. Gordon, Princeton University Press, Princeton, NJ, 1976.
Physical Properties of Polymers, J.E. Mark et al., American Chemical Society, 1984.
Physicochemical Aspects of Protein Denaturation, S. Lapanje, Wiley-Interscience, New York, 1978.
Protein Functionality in Foods, J.P. Cherry ed., ACS Symposium Series 147, American Chemical Society, 1981.
Protein Quality and the Effects of Processing, R.D. Phillips and J.W. Finley eds., Marcel Dekker, New York, 1989.
Proteins, J.G. Kirkwood, Gordon and Breach, New York, 1967.
Rubber Technology, M. Morton ed., Van Nostrand, New York, 1973.
Rubber-Toughened Plastics, C.K. Riew ed., Advances in Chemistry 222, American Chemical Society, 1987.
The Testing and Inspection of Engineering Materials, H.E. Davis et al., McGraw-Hill, New York, 1964.
Ablett, R.F., Bligh, E.G., Spencer, K., “Influence of Freshness on Quality of White Hake (Urophycis-Tenuis) Surimi”, Can Inst Food Sci Technol J (1991) 24 36-41.
Ackers, G.K., “Binding and Linkage – Functional Chemistry of Biological Macromolecules, by J. Wyman, S.J. Gill”, Nature (1991) 349 377.
Acton, J.C., Dick, R.L., “Functional properties of raw materials water-binding, fat emulsion and protein gelation can be influenced by the meat’s tissue characteristics.”, Meat Industry (1985) 32-36.
Acton, J.C. Kropp, P.S. Dick, R.L., “Properties of Ovalbumin, Conalbumin, and Lysozyme at an Oil-Water Interface and in an Emulsion System”, Poultry Science (1990) 69 694-701.
Acton, J.C., Saffle, R.L., “Preblended and prerigor meat in sausage emulsions”, Food Technology (1969) 23 93-97.
Adachi, S., Imagi, J., Matsuno, R., “Model for Estimation of the Stability of Emulsions in a Cream Layer”, Biosci Biotechnol Biochem (1992) 56 495-498.
Aguilera, J.M., Kinsella, J.E., “Compression Strength of Dairy Gels and Microstructural Interpretation”, J Food Sci (1991) 56 1224-1228.
Akahane, Y. Shimizu, Y., “Effects of Setting Incubation on the Water-Holding Capacity of Salt-Ground Fish Meat and Its Heated Gel”, Nippon Suisan Gakkaishi (1990) 56 139-146.
Aljawad, L.S., Bowers, J.A., “Water-binding capacity of ground lamb-soy mixtures with different levels of water and salt and internal end-point temperatures”, J. Food Science (1988) 53 376-378,382.
Alloncle, M., Doublier, J.L., “Viscoelastic Properties of Maize Starch Hydrocolloid Pastes and Gels”, Food Hydrocolloid (1991) 5 455-467.
Alvarez, V.B., Ofoli, R.Y., Smith, D.M., “Protein Insolubilization and Starch Gelatinization of Mechanically Deboned Chicken Meat and Cornstarch During Twin-Screw Extrusion”, Poultry Sci (1992) 71 1087-1095.
Alvarez, V.B., Smith, D.M., Flegler, S., “Effect of Extruder Die Temperature on Texture and Microstructure of Restructured Mechanically Deboned Chicken and Corn Starch”, Food Struct (1991) 10 153-160.
Alvarez, V.B., Smith, D.M., Morgan, R.G., Booren, A.M., “Restructuring of Mechanically Deboned Chicken and Nonmeat Binders in a Twin-Screw Extruder”, J. Food Science (1990) 55 942-946.
Amend, T., Belitz, H.D., Moss, R., Resmini, P., “Microstructural Studies of Gluten and a Hypothesis on Dough Formation”, Food Struct (1991) 10 277-288.
Annaka, M., Tanaka, T., “Multiple Phases of Polymer Gels”, Nature (1992) 355 430-432.
Arntfield, S.D., Murray, E.D., Ismond, M.A.H., “Dependence of Thermal Properties As Well As Network Microstructure and Rheology on Protein Concentration for Ovalbumin and Vicilin”, J Texture Stud (1990) 21 191-212.
Arntfield, S.D., Murray, E.D., Ismond, M.A.H., “Influence of Protein Charge on Thermal Properties As Well As Microstructure and Rheology of Heat Induced Networks for Ovalbumin and Vicilin”, J Texture Stud (1990) 21 295-322.
Arntfield, S.D., Murray, E.D., Ismond, M.A.H., “Role of Disulfide Bonds in Determining the Rheological and Microstructural Properties of Heat-Induced Protein Networks from Ovalbumin and Vicilin”, J Agr Food Chem (1991) 39 1378-1385.
Arntfield, S.D., Murray, E.D., “Heating Rate Affects Thermal Properties and Network Formation for Vicilin and Ovalbumin at Various pH Values”, J Food Sci (1992) 57 640-646.
Arteaga, G.E., Nakai, S., “Thermal Denaturation of Turkey Breast Myosin Under Different Conditions – Effect of Temperature and pH, and Reversibility of the Denaturation”, Meat Sci (1992) 31 191-200.
Autio, K., Kiesvaara, M., Malkki, Y., Kanko, S., “Chemical and functional properties of blood globin prepared by a new method”, J. Food Science (1984) 49 859-862.
Autio, K., Mietsch, F., “Heat-Induced Gelation of Myofibrillar Proteins and Sausages – Effect of Blood Plasma and Globin”, J. Food Science (1990) 55 1494.
Babak, V.G., “Principles of Stabilization of Emulsion Films and Highly Concentrated Emulsions by Adsorption Layers of Macromolecules”, Food Hydrocolloid (1992) 6 45-68.
Babbitt, J.K., Reppond, K.D., “Factors affecting the gel properties of surimi”, J. Food Science (1988) 53 965-966.
Barbut, S., Mittal, G.S., “Effect of Heat Processing Delay on the Stability of Poultry Meat Emulsions Containing 1.5 and 2.5 Percent Salt”, Poultry Sci (1991) 70 2538-2543.
Barbut, S. Mittal, G.S., “Effect of Heating Rate on Meat Batter Stability, Texture and Gelation”, Journal of Food Science (1990) 55 334-337.
Barbut, S., Mittal, G.S., “Influence of the Freezing Rate on the Rheological and Gelation Properties of Dark Poultry Meat”, POULTRY SCI (1990) 69 827-832.
Barbut, S., Mittal, G.S., “Rheological and gelation properties of meat batters prepared with three chloride salts”, J. Food Science (1988) 53 1296-1299,1311.
Barbut, S., “Effects of 3 Chopping Methods on Bologna Characteristics”, Can Inst Food Sci Technol J (1990) 23 149-153.
Barfod, N.M. Pedersen, K.S., “Determining the Setting Temperature of High-Methoxyl Pectin Gels”, Food Technology (1990) 44 139.
Bater, B., Maurer, A.J., “Effects of Fat Source and Final Comminution Temperature on Fat Particle Dispersion, Emulsion Stability, and Textural Characteristics of Turkey Frankfurters”, Poultry Sci (1991) 70 1424-1429.
Beas, V.E., Wagner, J.R., Anon, M.C., Crupkin, M., “Thermal Denaturation in Fish Muscle Proteins During Gelling – Effect of Spawning Condition”, J Food Sci (1991) 56 281-284.
Becher, P., “Food Emulsions – An Introduction”, Microemulsions and Emulsions (1991) 448 1-6.
Bernes, A., Galoux, M., “CIPAC Collaborative Study to Test a Colorimetric Method for Determination of the Stability of Dilute Emulsions”, Pestic Sci (1991) 32 173-185.
Beuschel, B.C., Culbertson, J.D., Partridge, J.A., Smith, D.M., “Gelation and Emulsification Properties of Partially Insolubilized Whey Protein Concentrates”, J Food Sci (1992) 57 605.
Biliaderis, C.G., Tonogai, J.R., “Influence of Lipids on the Thermal and Mechanical Properties of Concentrated Starch Gels”, J Agr Food Chem (1991) 39 833-840.
Biliaderis, C.G., Zawistowski, J., “Viscoelastic Behavior of Aging Starch Gels – Effects of Concentration, Temperature, and Starch Hydrolysates on Network Properties”, Cereal Chem (1990)67 240-246.
Bloukas, I., Honikel, K.O., “The Influence of Additives on the Oxidation of Pork Back Fat and Its Effect on Water and Fat Binding in Finely Comminuted Batters”, Meat Sci (1992) 32 31-43.
Bloukas, I., Honikel, K.O., “The Influence of Mincing and Temperature of Storage on the Oxidation of Pork Back Fat and Its Effect on Water-Binding and Fat-Binding in Finely Comminuted Batters”, Meat Sci (1992) 32 215-227.
Boles, J.A., Parrish, F.C., Huiatt, T.W., Robson, R.M., “Effect of Porcine Stress Syndrome on the Solubility and Degradation of Myofibrillar Cytoskeletal Proteins”, J Anim Sci (1992) 70 454-464.
Borisova, M.A., Oreshkin, E.F., “On the Water Condition in Pork Meat”, Meat Sci (1992) 31 257-265.
Borissowa, M.A., Iwaschow, W.I., Oreschkin, E.F., Chursin, A.B., “The Influence of Polyphosphates on the Water Binding of Meat from Different Quality Groups”, Fleischwirtschaft (1991) 71 202-204.
Borton, R.J., Webb, N.B., Bratzler, L.J., “Emulsifying capacities and emulsion stability of dilute meat slurries from various meat trimmings”, Food Technology (1968) 22 162-164.
Bracho, G.E., Haard, N.F., “Determination of Collagen Crosslinks in Rockfish Skeletal Muscle”, J Food Biochem (1990) 14 435-451.
Interfacial Areas in Emulsions Using Turbidimetric and Droplet Size Data – Correction of the Formula for Emulsifying Activity Index”, J Agr Food Chem (1991) 39 655-659.
Camou, J.P., Sebranek, J.G., “Gelation Characteristics of Muscle Proteins from Pale, Soft, Exudative (PSE) Pork”, Meat Sci (1991) 30 207-220.
Campbell, J.F., “Stability of meat emulsions affected by the form of sodium chloride used”, Meat Industry (1980) 56-57.
Cao, Y.H., Dickinson, E., Wedlock, D.J., “Influence of Polysaccharides on the Creaming of Casein-Stabilized Emulsions”, Food Hydrocolloid (1991) 5 443-454.
Carbonell, E., Costell, E., Duran, L., “Fruit Content Influence on Gel Strength of Strawberry and Peach Jams”, J Food Sci (1991) 56 1384-1387.
Carpenter, J.A., Saffle, R.L., Christian, J.A., “The effect of type of meat and levels of fat on organoleptic and other qualities of frankfurters”, Food Technology (1966) 20 125-127.
Carpenter, J.A., Saffle, R.L., “A simple method of estimating the emulsifying capacity of various sausage meats”, J. Food Science (1964) 29 774-781.
Carpenter, J.A., Saffle, R.L., “Some physical and chemical factors affecting the emulsifying capacity of meat protein extracts”, Food Technology (1965) 19 111-115.
Carrillo, A.R., Kokini, J.L., “Effect of egg yolk and egg yolk + salt on rheological properties and particle size distribution of model oil-in-water salad dressing emulsions”, J. Food Science (1988) 53 1352-1355,1366.
Carroll, R.J., Lee, C.M., “Meat emulsions – fine structure relationships and stability”, Scanning Electron Microscopy (1981) 3 105-110.
Castelain, C., Bronnec, I., Genot, C., Laroche, M., “Flow Behavior and Stability of Concentrated Oil-in-Water Emulsions – Effects of Modified Starch in Aqueous Phase”, Sci Aliment (1990) 10 453-463.
Causeret, D., Matringe, E., Lorient, D., “Ionic Strength and pH Effects on Composition and Microstructure of Yolk Granules”, J Food Sci (1991) 56 1532-1536.
Chacon, E.J.G., Satterlee, L.D., Hanna, M.A., “Heat Induced Gels from Partially Hydrolyzed Soy Protein Isolate”, Journal of Food Biochemistry (1990) 14 15-29.
Chai, E., Oakenfull, D.G., Mcbride, R.L., Lane, A.G., “Sensory Perception and Rheology of Flavoured Gels”, Food Aust (1991) 43 256.
Chalmers, M., Careche, M., Mackie, I.M., “Properties of Actomyosin Isolated from Cod (Gadus morhua) After Various Periods of Storage in Ice”, J Sci Food Agr (1992) 58 375-383.
Champagne, E.T., Marshall, W.E., Goynes, W.R., “Effects of Degree of Milling and Lipid Removal on Starch Gelatinization in the Brown Rice Kernel”, Cereal Chem (1990) 67 570-574.
Chang, S.M., Liu, L.C., “Retrogradation of Rice Starches Studied by Differential Scanning Calorimetry and Influence of Sugars, NaCl and Lipids”, J Food Sci (1991) 56 564.
Chen, C.M., Trout, G.R., “Color and Its Stability in Restructured Beef Steaks During Frozen Storage – Effects of Various Binders”, J Food Sci (1991) 56 1461.
Chen, C.M., Trout, G.R., “Sensory, Instrumental Texture Profile and Cooking Properties of Restructured Beef Steaks Made with Various Binders”, J Food Sci (1991) 56 1457-1460.
Chen, J.Y., Piva, M., Labuza, T.P., “Evaluation of water binding capacity (WBC) of food fiber sources”, J. Food Science (1984) 49 59-63.
Chiba, K. Tada, M., “Relationship Between the Emulsion Stability and Phospholipid Distribution in the Aqueous Phases Inside and Outside of an Emulsion Droplet”, Agricultural and Biological Chemistry (1990) 54 907-912.
Chinachoti, P., Kimshin, M.S., Mari, F., Lo, L., “Gelatinization of Wheat Starch in the Presence of Sucrose and Sodium Chloride – Correlation Between Gelatinization Temperature and Water Mobility As Determined by Oxygen-17 Nuclear Magnetic Resonance”, Cereal Chem (1991) 68 245-248.
Chinachoti, P. Steinberg, M.P. Villota, R., “A Model for Quantitating Energy and Degree of Starch Gelatinization Based on Water, Sugar and Salt Contents”, Journal of Food Science (1990) 55 543-546.
Chinachoti, P., White, V.A., Lo, L., Stengle, T.R., “Application of High-Resolution Carbon-13, Oxygen-17, and Sodium-23 Nuclear Magnetic Resonance to Study the Influences of Water, Sucrose, and Sodium Chloride on Starch Gelatinization”, Cereal Chem (1991) 68 238-244.
Choe, I.S., Morita, J.I., Yamamoto, K., Samejima, K., Yasui, T., “Heat-Induced Gelation of Myosins/Subfragments from Chicken Leg and Breast Muscles at High Ionic Strength and Low pH”, J Food Sci (1991) 56 884-890.
Chrastil, J., “Gelation of Calcium Alginate – Influence of Rice Starch or Rice Flour on the Gelation Kinetics and on the Final Gel Structure”, J Agr Food Chem (1991) 39 874-876.
Chrastil, J., “Influence of Storage on Supercooling of Rice Starch and Flour Gels”, J Agr Food Chem (1991) 39 1729-1731.
Christian, J.A., Saffle, R.L., “Plant and animal fats and oils emulsified in a model system with muscle salt-soluble protein”, Food Technology (1967) 21 86-89.
Chung, K.H., Lee, C.M., “Relationships Between Physicochemical Properties of Nonfish Protein and Textural Properties of Protein-Incorporated Surimi Gel”, J. Food Science (1990) 55 972.
Chung, K.H., Lee, C.M., “Water Binding and Ingredient Dispersion Pattern Effects on Surimi Gel Texture”, J Food Sci (1991) 56 1263-1266.
Chung, S.L., Ferrier, L.K., “pH and Sodium Chloride Effects on Emulsifying Properties of Egg Yolk Phosvitin”, J Food Sci (1992) 57 40-42.
Colmenero, F.J., Carballo, J., Cofrades, S., “Effect of Freezing and Frozen Storage on the Aromatic Hydrophobicity of Pork Myosin”, Z Lebensmittel-Untersuch Fors (1991) 193 441-444.
Condepetit, B., Escher, F., “Gelation of Low Concentration Starch Systems Induced by Starch Emulsifier Complexation – Short Communication”, Food Hydrocolloid (1992) 6 223-229.
Correia, L.R., Mittal, G.S., Usborne, W.R., “Selection Criteria of Meat Emulsion Fillers Based on Properties and Cooking Kinetics”, J Food Sci (1991) 56 380-386.
Correia, L.R., Mittal, G.S., “Kinetics of Hydration Properties of Meat Emulsions Containing Various Fillers During Smokehouse Cooking”, Meat Science (1991) 29 335-351.
Correia, L.R., Mittal, G.S., “Kinetics of pH and Colour of Meat Emulsions Containing Various Fillers During Smokehouse Cooking”, Meat Science (1991) 29 353-364.
Creamer, L.K., “Some Aspects of Casein Micelle Structure”, Interactions of Food Proteins (1991) 454 148-163.
Curran, D.M., Tepper, B.J., Montville, T.J., “Use of Bicarbonates for Microbial Control and Improved Water-Binding Capacity in Cod Fillets”, J. Food Science (1990) 55 1564-1566.
Dahme, A., “Gelpoint Measurements on High-Methoxyl Pectin Gels by Different Techniques”, J Texture Stud (1992) 23 1-11.
Dalgleish, D.G., Horne, D.S., “Studies of Gelation of Acidified and Renneted Milks Using Diffusing Wave Spectroscopy”, Milchwissenschaft (1991) 46 417.
Damasio, M.H., Capilla, C., Costell, E., Duran, L., “Influence of Composition on Mechanical Properties of Kappa-Carrageenan, Locust Bean Gum, Guar Gum Mixed Gels – Resistance to Cut”, REV AGROQUI (1990) 30 254-265.
Damasio, M.H. Capilla, C. Costell, E. Duran,L., “Influence of Composition on Mechanical Properties of Kappa-Carrageenan, Locust Bean Gum, Guar Gum, Mixed Gels – Puncture and Penetration Tests”, Revista de Agroquimica Y Tecnologia de Alimentos (1990) 30 109-121.
Deng, J.C., Toledo, R.T., Lillard, D.A., “Protein-protein interaction and fat and water binding in comminuted flesh products”, J. of Food Science (1981) 46 1117-1121.
Dickinson, E., Evison, J., Owusu, R.K., “Preparation of Fine Protein-Stabilized Water-in-Oil-in-
Water Emulsions”, Food Hydrocolloid (1991) 5 481-485.
Dickinson, E., Galazka, V.B., Anderson, D.M.W., “Emulsifying Behaviour of Gum Arabic .1. Effect of the Nature of the Oil Phase on the Emulsion Droplet-Size Distribution”, Carbohyd Polym (1991) 14 373-383.
Dickinson, E., Galazka, V.B., Anderson, D.M.W., “Emulsifying Behaviour of Gum Arabic .2. Effect of the Gum Molecular Weight on the Emulsion Droplet-Size Distribution”, Carbohyd Polym (1991) 14 385-392.
Dickinson, E., Stainsby, G., “Progress in the formulation of food emulsions and foams”, Food Technology (1987) 74-81.
Dickinson, E., Tanai, S., “Protein Displacement from the Emulsion Droplet Surface by Oil-Soluble and Water-Soluble Surfactants”, J Agr Food Chem (1992) 40 179-183.
Dickinson, E., Tanai, S., “Temperature Dependence of the Competitive Displacement of Protein from the Emulsion Droplet Surface by Surfactants”, Food Hydrocolloid (1992) 6 163-171.
Dickinson, E., “Competitive Adsorption and Protein Surfactant Interactions in Oil-in-Water Emulsions”, Microemulsions and Emulsions (1991) 448 114-129.
Dymsza, H.A., Lee, C.M., Saibu, L.O., Haun, J., Silverman, G.J., Josephson, E.S., “Gamma Irradiation Effects on Shelf Life and Gel Forming Properties of Washed Red Hake (Urophycis-Chuss) Fish Mince”, J. Food Science (1990) 55 1745.
Eerd, J.P., “Emulsion stability and protein extractability of ovine muscle as a function of time postmortem”, J. of Food Science (1972) 37 473-475.
Egelandsdal, B., Fretheim, K., Harbitz, O., Hermansson, A., “Causes for the increase in moisture loss from comminuted heat-treated meat mixtures containing added lecithin”, Fleischwirtsch International (1989) 3 43-47.
Eliasson, A.C., “A Calorimetric Investigation of the Influence of Sucrose on the Gelatinization of Starch”, Carbohyd Polym (1992) 18 131-138.
Elizalde, B.E., De Kanterwicz, R.J., Pilosof, A.M.R., Bartholomai, G.B., “Physicochemical properties of food proteins related to their ability to stabilize oil-in-water emulsions”, J. Food Science (1988) 53 845-848.
Elizalde, B.E., Pilosof, A.M.R., Bartholomai, G.B., “Prediction of Emulsion Instability from Emulsion Composition and Physicochemical Properties of Proteins”, J. Food Science (1991) 56 116-120.
Elizalde, B.E., Pilosof, A.M.R., Bartholomai, G.B., “Relationship of Absorptive and Interfacial Behavior of Some Food Proteins to Their Emulsifying Properties”, J. Food Science (1991) 56 253-254.
Ensor, S.A., Mandigo, R.W., Calkins, C.R., Quint, L.N., “Comparative evaluation of whey protein concentrate, soy protein isolate and calcium-reduced nonfat dry milk as binders in an emulsion-type sausage”, J. Food Science (1987) 52 1155-1158.
Ensor, S.A., Sofos, J.N., Schmidt, G.R., “Differential Scanning Calorimetric Studies of Meat Protein-Alginate Mixtures”, J. Food Science (1991) 56 175.
Evans, I.D., Lips, A., “Viscoelasticity of Gelatinized Starch Dispersions”, J Texture Stud (1992) 23 69-86.
Fanta, G.F., Christianson, D.D., “Influence of Poly(Ethylene-Co-Acrylic Acid) on the Paste Viscosity and Gel Rheology of Cornstarch Dispersions”, Cereal Chem (1991) 68 300-304.
Fernandes, P.B., Goncalves, M.P., Doublier, J.L., “A Rheological Characterization of Kappa-Carrageenan Galactomannan Mixed Gels – A Comparison of Locust Bean Gum Samples”, Carbohyd Polym (1991) 16 253-274.
Fiszman, S.M., Duran, L., “Effects of Fruit Pulp and Sucrose on the Compression Response of Different Polysaccharides Gel Systems”, Carbohyd Polym (1992) 17 11-17.
Fligner, K.L., Mangino, M.E., “Relationship of Composition to Protein Functionality”, Interactions of Food Proteins (1991) 454 1-2.
Foegeding, E.A., Brekke, C.J., Xiong, Y.L., “Gelation of Myofibrillar Protein”, Interactions of Food Proteins (1991) 454 257-267.
Foegeding, E.A., Ramsey, S.R., “Rheological and water-holding properties of gelled meat batters containing iota carrageenan, kappa carrageenan or xanthaan gum”, J. Food Science (1987) 52 549-553.
Foegeding, E.A., “Development of a Test to Predict Gelation Properties of Raw Turkey Muscle Proteins”, J. Food Science (1990) 55 932.
Frauenfelder, H., Sligar, S.G., Wolynes, P.G., “The Energy Landscapes and Motions of Proteins”, Science (1991) 254 1598-1603.
Friberg, S.E., Kayali, I., “Surfactant Association Structures, Microemulsions, and Emulsions in Foods – An Overview”, Microemulsions and Emulsions (1991) 448 7-24.
Galluzzo, S.J., Regenstein, J.M., “Emulsion capacity and timed emulsification of chicken breast muscle myosin”, J. of Food Science (1978) 43 1757-1760.
Galluzzo, S.J., Regenstein, J.M., “Role of chicken breast muscle proteins in meat emulsion formation: myosin, actin and synthetic actomyosin”, J. of Food Science (1978) 43 1761-1765.
Galluzzo, S.J., Regenstein, J.M., “Role of chicken breast muscle proteins in meat emulsion formation: natural actomyosin, contracted and uncontracted myofibrils”, J. of Food Science (1978) 43 1766-1770.
Gaonkar, A.G., “Surface and Interfacial Activities and Emulsion Characteristics of Some Food Hydrocolloids”, Food Hydrocolloid (1991) 5 329-337.
Gault, P., Mahaut, M., Korolczuk, J., “Rheological Characterization and Heat Gelation of Whey Protein Concentrate”, LAIT (1990) 70 217-232.
Gekko, K., Fukamizu, M., “Effect of Pressure on the Sol-Gel Transition of Agarose”, Agr Biol Chem Tokyo (1991) 55 2427-2428.
Gillett, T.A., Meiburg, D.E., Brown, C.L., Simon, S., “Parameters affecting meat protein extraction and interpretation of model system data for meat emulsion formation”, J. Food Science (1977) 42 1606-1610.
Gilson, C.D., Thomas, A., Hawkes, F.R., “Gelling Mechanism of Alginate Beads with and Without Immobilised Yeast”, Process Biochem (1990) 25 104-108.
Goloubinoff, P., Gatenby, A.A., Lorimer, G.H., “Role of Chaperonins in Protein Folding”, Protein Refolding (1991) 470 110-118.
Gordon, A., Barbut, S., “Effect of Chemical Modifications on the Microstructure of Raw Meat Batters”, Food Struct (1991) 10 241-253.
Gordon, A., Barbut, S., “Effect of Chloride Salts on Protein Extraction and Interfacial Protein Film Formation in Meat Batters”, J Sci Food Agr (1992) 58 227-238.
Gordon, A., Barbut, S., “Raw Meat Batter Stabilization – Morphological Study of the Role of Interfacial Protein Film”, Can Inst Food Sci Technol J (1991) 24 136-142.
Gordon, A., Barbut, S., “The Microstructure of Raw Meat Batters Prepared with Monovalent and Divalent Chloride Salts”, Food Struct (1990) 9 279-295.
Gordon, A., Barbut, S., “The Role of the Interfacial Protein Film in Meat Batter Stabilization”, Food Struct (1990) 9 77-90.
Gossett, P.W., Rizvi, S.S.H., Baker, R.C., “Quantitative analysis of gelation in egg protein systems”, Food Technology (1984) 67-74.
Harada, T., Kanzawa, Y., Kanenaga, K., Koreeda, A., Harada, A., “Electron Microscopic Studies on the Ultrastructure of Curdlan and Other Polysaccharides in Gels Used in Foods – Review Paper”, Food Struct (1991) 10 1-18.
Hargus, G.L., Froning, G.W., Mebus, C.A., Neelakantan, S., Hartung, T.E., “Effect of processing variables on stability and protein extractability of turkey meat emulsions”, J. of Food Science (1970)35 688-692.
Hartnett, E.K., Satterlee, L.D., “The Formation of Heat and Enzyme Induced (Plastein) Gels from Pepsin-Hydrolyzed Soy Protein Isolate”, Journal of Food Biochemistry (1990) 14 1-13.
Hasegawa, M., Kitano, H., “The Effect of Pore-Size Distribution on the Binding of Proteins to Porous Resin Beads”, Biotechnol Bioeng (1991) 37 608-613.
Hastings, R.J., Keay, J.N., Young, K.W., “The Properties of Surimi and Kamaboko Gels from 9 British Species of Fish”, INT J FOOD (1990) 25 281-294.
Hatanaka, C., Sakamoto, K., Wada, Y., “Preparation of a Water-Insoluble Hard Gel, Crosslinked Cell Walls, from Citrus Peels”, Agr Biol Chem Tokyo (1990) 54 3347-3348.
Hayashi, A. Takazawa, H. Saika, M., “Heat-Induced Gelation of Human Serum Albumin and Model Compounds”, Agricultural and Biological Chemistry (1990) 54 1121-1127.
Hennigar, C.J., Buck, E.M., Hultin, H.O., Peleg, M., Vareltzis, K., “Effect of washing and sodium chloride on mechanical properties of fish muscle gels”, J. Food Science (1988) 53 963- 964.
Hermansson, A.M., Akesson, C., “Functional properties of added proteins correlated with properties of meat systems. Effect of concentration and temperature on water-binding properties of model meat systems”, J. of Food Science (1975) 40 595-602.
Hermansson, A.M., Akesson, C., “Functional properties of added proteins correlated with properties of meat systems. Effect of salt on wate-binding properties model meat systems”, J. of Food Science (1975) 40 603-610.
Hermansson, A.M., Eriksson, E., Jordansson, E., “Effects of Potassium, Sodium and Calcium on the Microstructure and Rheological Behaviour of Kappa-Carrageenan Gels”, Carbohyd Polym (1991) 16 297-320.
Hermansson, A.M., Lucisano, M., “Gel characteristics-waterbinding properties of blood plasma gels and methodological aspects on the waterbinding of gel systems”, J. of Food Science (1982) 47 1955-1959,1964.
Hermansson, A.M., “Gel characteristics-compression and penetration of blood plasma gels”, J. of Food Science (1982) 47 1960-1964.
Hermansson, A.M., “Gel characteristics-structure as related to texture and waterbinding of blood plasma gels”, J. of Food Science (1982) 47 1965-1972.
Hirahara, H. Tanaka, M. Nagashima, Y. Taguchi, T., “Thermal Gelation of Striped Marlin and Sardine Myosins”, Nippon Suisan Gakkaishi (1990) 56 545.
Hirose, M., Nishizawa, Y., Lee, J.Y., “Gelation of Bovine Serum Albumin by Glutathione”, J. Food Science (1990) 55 915.
Holcomb, D.N., Pechak, D.G., Chakrabarti, S., Opsahl, A., “Visualizing Textural Changes in Dairy Products by Image Analysis”, Food Technol (1992) 46 122.
Holt, D.L., Watson, M.A., Dill, C.W., Alford, E.S., Edwards, R.L., Diehl, K.C., Gardner, F.A., “Correlation of the rheological behavior of egg albumen to temperature, pH and NaCl concentration”, J. Food Science (1984) 49 137-141.
Horiuchi, H., “Dynamic Properties of Elastic Modulus in Some Heterogeneous Gels”, J Texture Stud (1990) 21 141-154.
Horton, S.D., Lauer, G.N., White, J.S., “Predicting Gelatinization Temperatures of Starch Sweetener Systems for Cake Formulation by Differential Scanning Calorimetry .2. Evaluation and Application of a Model”, Cereal Food World (1990) 35 734.
Hoshi, Y., “Effect of Moisture Sorption on Gelation of Commercial Soy Protein Isolate”, J Jpn Soc Food Sci Technol (1991) 38 411-413.
Hsieh, F., Peng, I.C., Clarke, A.D., Mulvaney, S.J., Huff, H.E., “Restructuring of Mechanically Deboned Turkey by Extrusion Processing Using Cereal Flours As the Binder”, Food Sci Technol-Lebensm Wiss (1991) 24 139-144.
Huber, D.G., Regenstein, J.M., “Emulsion stability studies of myosin and exhaustively washed muscle from adult chicken breast muscle”, J. Food Science (1988) 53 1282-1286,1293.
Hung, S.C., Zayas, J.F., “Emulsifying Capacity and Emulsion Stability of Milk Proteins and Corn Germ Protein Flour”, J Food Sci (1991) 56 1216.
Ilmain, F., Tanaka, T., Kokufuta, E., “Volume Transition in a Gel Driven by Hydrogen Bonding”, Nature (1991) 349 400-401.
Inada, N., Ichikawa, H., Nozaki, Y., Hiraoka, K., Yokoyama, T., Tabata, Y., “Effects of Sugars on Hydration and Denaturation of Fish Myofibrillar Protein Due to Dehydration with Silica Gel”, J Jpn Soc Food Sci Technol (1992) 39 211-218.
Ivey, F.J., Webb, N.B., Jones, V.A., “The effect of disperse phase droplet size and interfacial film thickness on the emulsifying capacity and stability of meat emulsions”, Food Technology (1970) 24 91-93.
Janas, P., “Rheological Studies on Potato Starch Pastes at Low Concentrations .4. Absolute Measurements of the Rheological Properties of Starch During Gelatinization”, Starch (1991) 43 172-175.
Janmey, P.A. Hvidt, S. Lamb, J. Stossel, T.P., “Resemblance of Actin-Binding Protein Actin Gels to Covalently Crosslinked Networks”, Nature (1990) 345 89-92.
Janmey, P.A., Hvidt, S., Oster, G.F., Lamb, J., Stossel, T.P., Hartwig, J.H., “Effect of ATP on Actin Filament Stiffness”, Nature (1990) 347 95-99.
Janssen, F.W., Hagele, G.H., Voorpostel, A.M.B., Debaaij, J.A., “Myoglobin Analysis for Determination of Beef, Pork, Horse, Sheep, and Kangaroo Meat in Blended Cooked Products”, J. Food Science (1990) 55 1528.
Jansson, K.W., Lindahl, L., “Rheological Changes in Oatmeal Suspensions During Heat Treatment”, J Food Sci (1991) 56 1685-1689.
Ji, E.S., Lee, J.Y., Hirose, M., “Thiol-Dependent Gelation of Bovine Serum Albumin in the Presence of Ethanol”, Agr Biol Chem Tokyo (1991) 55 861-862.
Johnson, H.R., “Physical and chemical influences on meat emulsion stability”, Food Technology (1975) 167.
Jorgensen, W.L., “Rusting of the Lock and Key Model for Protein-Ligand Binding”, Science (1991) 254 954-955.
Kajiwara, K., Rossmurphy, S.B., “Polymers – Synthetic Gels on the Move”, Nature (1992) 355 208-209.
Kamata, Y. Umeya, J. Kimura, M. Tanii, S. Yamauchi, F., “Effects of Heating Rate and High-Temperature Holding on Soy Protein Gel Viscosity”, Journal of the Japanese Society for Food Science and Technol (1990) 37 184-190.
Kaminishi, Y., Miki, H., Isohata, T., Nishimoto, J., “Effect of Temperature on Reactions of Heat-Induced Gel Formation in Smooth Dogfish Muscle”, Nippon Suisan Gakkaishi (1990) 56 1285-1292.
Kang, I.J., Matsumura, Y., Mori, T., “Characterization of Texture and Mechanical Properties of Heat-Induced Soy Protein Gels”, J Amer Oil Chem Soc (1991) 68 339-345.
Kato, A., Ibrahim, H.R., Takagi, T., Kobayashi, K., “Excellent Gelation of Egg White Preheated in the Dry State Is Due to the Decreasing Degree of Aggregation”, J Agr Food Chem (1990) 38 1868-1872.
Katsuta, K., Kinsella, J.E., “Effects of Temperature on Viscoelastic Properties and Activation Energies of Whey Protein Gels”, J. Food Science (1990) 55 1296-1302.
Katsuta, K., Kinsella, J.E., “Spontaneous Gelation of Whey Proteins in Urea and Guanidine Hydrochloride”, Agr Biol Chem Tokyo (1990) 54 2423-2424.
Katsuta, K. Rector, D. Kinsella, J.E., “Viscoelastic Properties of Whey Protein Gels – Mechanical Model and Effects of Protein Concentration on Creep”, Journal of Food Science (1990) 55 516-521.
Ker, Y.C., Toledo, R.T., “Influence of Shear Treatments on Consistency and Gelling Properties of Whey Protein Isolate Suspensions”, J Food Sci (1992) 57 82.
Kim, B.Y., Hamann, D.D., Lanier, T.C., Wu, M.C., “Effects of freeze-thaw abuse on the viscosity and gel-froming properties of surimi from two species”, J. Food Science (1986) 51 951-956,1004.
Kim, C.S., Walker, C.E., “Effects of Sugars and Emulsifiers on Starch Gelatinization Evaluated by Differential Scanning Calorimetry”, Cereal Chem (1992) 69 212-217.
Kim, C.S., Walker, C.E., “Interactions Between Starches, Sugars, and Emulsifiers in High-Ratio Cake Model Systems”, Cereal Chem (1992) 69 206-212.
Kimura, I., Sugimoto, M., Toyoda, K., Seki, N., Arai, K., Fujita, T., “A Study on the Cross-Linking Reaction of Myosin in Kamaboko Suwari Gels”, Nippon Suisan Gakkaishi (1991) 57 1389-1396.
Klemaszewski, J.L., Kinsella, J.E., “Sulfitolysis of Whey Proteins – Effects on Emulsion Properties”, J Agr Food Chem (1991) 39 1033-1036.
Kneifel, W., Paquin, P., Abert, T., Richard, J.P., “Water-Holding Capacity of Proteins with Special Regard to Milk Proteins and Methodological Aspects – A Review”, J Dairy Sci (1991) 74 2027-2041.
Knipe, C.L., Olson, D.G., Rust, R.E., “Effects of inorganic phosphates and sodium hydroxide on the cooked cured color, ph and emulsion stability of reduced-sodium and conventional meat emulsions”, J. Food Science (1981) 53 1305-1308.
Knutson, C.A., “Annealing of Maize Starches At Elevated Temperatures”, Cereal Chem (1990) 67 376-384.
Ko, W.C., Tanaka, M., Nagashima, Y., Taguchi, T., Amano, K., “Effect of High Pressure
Treatment on the Thermal Gelation of Sardine and Alaska Pollack Meat and Myosin Pastes”, J Jpn Soc Food Sci Technol (1990) 37 637-642.
Kohyama, K., Nishinari, K., “Cellulose Derivatives Effects on Gelatinization and Retrogradation of Sweet Potato Starch”, J Food Sci (1992) 57 128.
Kohyama, K., Nishinari, K., “Effect of Soluble Sugars on Gelatinization and Retrogradation of Sweet Potato Starch”, J Agr Food Chem (1991) 39 1406-1410.
Kohyama, K., Yoshida, M., Nishinari, K., “Rheological Study on Gelation of Soybean-11S Protein by Glucono-delta-Lactone”, J Agr Food Chem (1992) 40 740-744.
Kolakowski, E., Wianecki, M., “Thermal Denaturation and Aggregation of Proteins in Minced Fish As Studied by a Thermomechanical Method”, J. Food Science (1990) 55 1477.
Konno, A., Harada, T., “Thermal Properties of Curdlan in Aqueous Suspension and Curdlan Gel”, Food Hydrocolloid (1991) 5 427-434.
Koohmaraie, M., Kennick, W.H., Anglemier, A.F., Elgasim, E.A., Jones, T.K., “Effect of postmortem storage on cold-shortened bovine muscle: analysis by SDS-polyacrlamide gel electrophoresis”, J. Food Science (1984) 49 290-291.
Koohmaraie, M., Kennick, W.H., Elgasim, E.A., Anglemier, A.F., “Effects of postmortem storage on muscle protein degradation: analysis by SDS-polyacrylamide gel electrophoresis”, J. Food Science (1984) 49 292-293.
Kratzer, F.H. Bersch, S. Vohra, P., “Evaluation of Heat-Damage to Protein by Coomassie Blue G Dye-Binding”, Journal of Food Science (1990) 55 805-807.
Krog, N., Larsson, K., “Crystallization at Interfaces in Food Emulsions – A General Phenomenon”, Fett Wiss Technol (1992) 94 55-57.
Krog, N., “Thermodynamics of Interfacial Films in Food Emulsions”, Microemulsions and Emulsions (1991) 448 138-145.
Kuhn, P.R., Foegeding, E.A., “Factors Influencing Whey Protein Gel Rheology – Dialysis and Calcium Chelation”, J Food Sci (1991) 56 789-791.
Kuhn, P.R., Foegeding, E.A., “Mineral Salt Effects on Whey Protein Gelation”, J Agr Food Chem (1991) 39 1013-1016.
Kulicke, W.M. Aggour, Y.A. Elsabee, M.Z., “Preparation, Characterisation, and Rheological Behaviour of Starch-Sodium Trimetaphosphate Hydrogels”, Starch-Starke (1990) 42 134-141.
Ladwig, K.M., Knipe, C.L., Sebranek, J.G., “Effects of collagen and alkaline phosphate on time of chopping, emulsion stability and protein solubility of finecut meat systems”, J. of Food Science (1989) 00 541-544.
Laligant, A., Dumay, E., Valencia, C.C., Cuq, J.L., Cheftel, J.C., “Surface Hydrophobicity and Aggregation of beta-Lactoglobulin Heated Near Neutral pH”, J Agr Food Chem (1991) 39 2147-2155.
Langton, M., Hermansson, A.M., “Fine-Stranded and Particulate Gels of beta-Lactoglobulin and Whey Protein at Varying pH”, Food Hydrocolloid (1992) 5 523-539.
Lanier, T.C., “Interactions of Muscle and Nonmuscle Proteins Affecting Heat-Set Gel Rheology”, Interactions of Food Proteins (1991) 454 268-284.
Larsson, I., Eliasson, A.C., “Annealing of Starch at an Intermediate Water Content”, Starch (1991) 43 227-231.
Larsson, K., “Emulsions of Reversed Micellar Phases and Aqueous Dispersions of Cubic Phases of Lipids – Some Food Aspects”, Microemulsions and Emulsions (1991) 448 44-50.
Latreille, B., Paquin, P., “Evaluation of Emulsion Stability by Centrifugation with Conductivity Measurements”, J. Food Science (1990) 55 1666.
Leblanc, E.L., Leblanc, R.J., “Determination of Hydrophobicity and Reactive Groups in Proteins of Cod (Gadus-Morhua) Muscle During Frozen Storage”, Food Chem (1992) 43 3-11.
Lee, C.M., Abdollahi, A., “Effect of hardness of plastic fat on structure and material properties of fish protein gels”, J. of Food Science (1981) 46 1755-1759.
Lee, C.M., Carroll, R.J., Abdollahi, A., “A microscopical study of the structure of meat emulsions and its relationship to thermal stability”, J. of Food Science (1981) 46 1789-1793,1804.
Lee, E.J., Chandrasekaran, R., “X-Ray and Computer Modeling Studies on Gellan-Related Polymers – Molecular Structures of Welan, S-657, and Rhamsan”, Carbohydr Res (1991) 214 11-24.
Lee, J.Y., Hirose, M., “Effect of Salts on the Thiol-Dependent Gelation of Bovine Serum Albumin”, Agr Biol Chem Tokyo (1991) 55 2057-2062.
Lee, N. Seki, N. Kato, N. Nakagawa, N. Terui, S. Arai, K., “Gel Forming Ability and Cross-Linking Ability of Myosin Heavy Chain in Salted Meat Paste from Threadfin Bream”, Nippon Suisan Gakkaishi-Bulletin of the Japanese Society of (1990) 56 329-336.
Lee, N.H., Kato, N., Nakagawa, N., Terui, S., Seki, N., Arai, K., “Characteristic Gelling Properties of Salt-Ground Meat from Jurel Surimi in Connection with Change in Myofibrillar Protein”, Nippon Suisan Gakkaishi (1991) 57 1193-1201.
Lee, N.H., Seki, N., Kato, N., Nakagawa, N., Terui, S., Arai, K., “Changes in Myosin Heavy Chain and Gel Forming Ability of Salt-Ground Meat from Hoki”, Nippon Suisan Gakkaishi (1990) 56 2093-2101.
Leloup, V.M., Colonna, P., Buleon, A., “Influence of Amylose Amylopectin Ratio on Gel Properties”, J Cereal Sci (1991) 13 1-13.
Leloup, V.M., Colonna, P., Ring, S.G., Roberts, K., Wells, B., “Microstructure of Amylose Gels”, Carbohyd Polym (1992) 18 189-197.
Lemeste, M., Closs, B., Courthaudon, J.L., Colas, B., “Interactions Between Milk Proteins and Lipids – A Mobility Study”, Interactions of Food Proteins (1991) 454 137-147.
Lemeste, M., Colas, B., Simatos, D., Closs, B., Courthaudon, J.L., Lorient, D., “Contribution of Protein Flexibility to the Foaming Properties of Casein”, J. Food Science (1990) 55 1445-1447.
Lesiow, T., “Comparison of Changes Occurring in Rheological Properties of Gelled Tissue and Model Sausage Prepared from Duck Breast Muscles Stored At-2-Degrees-C and -18-Degrees-C”, Nahrung (1990) 34 927-933.
Lesiow, T., “Influence of Storage Time of Duck Breast Muscles At -18-Degrees-C on Rheological Properties of Gelled Tissue and Model Sausage”, Nahrung (1990) 34 747-758.
Leszkowiat, M.J., Yada, R.Y., Coffin, R.H., Stanley, D.W., “Starch Gelatinization in Cold Temperature Sweetening Resistant Potatoes”, J. Food Science (1990) 55 1338.
Leuenberger, B.H., “Investigation of Viscosity and Gelation Properties of Different Mammalian and Fish Gelatins”, Food Hydrocolloid (1991) 5 353-361.
Lewis, D.F., “The use of microscopy to explain the behaviour of foodstuffs- a review of work carried out at the leatherhead food research association”, Scanning Electron Microscopy (1981) 3 25-37.
Lichan, E., Nakai, S., “Importance of Hydrophobicity of Proteins in Food Emulsions”, Microemulsions and Emulsions (1991) 448 193-212.
Lin, C.S, Zayas, J.F., “Microstuctural comparisons of meat emulsions prepared with corn protein emulsified and unemulsified fat”, J. Food Science (1987) 52 267-270.
Lin, S.W., Lakin, A.L., “Thermal Denaturation of Soy Proteins As Related to Their Dye-Binding Characteristics and Functionality”, J Amer Oil Chem Soc (1990) 67 872-878.
Liu, C.W., Huffman, D.L., Egbert, W.R., Liu, M.N., “Effects of Trimming and Added Connective Tissue on Compositional, Physical and Sensory Properties of Restructured, Pre-Cooked Beef Roasts”, J. Food Science (1990) 55 1258-1263.
Liu, H., Lelievre, J., Ayoungchee, W., “A Study of Starch Gelatinization Using Differential Scanning Calorimetry, X-Ray, and Birefringence Measurements”, Carbohydr Res (1991) 210 79-87.
Liu, H., Lelievre, J., “A Differential Scanning Calorimetry Study of Glass and Melting Transitions in Starch Suspensions and Gels”, Carbohydr Res (1991) 219 23-32.
Liu, H., Lelievre, J., “A Differential Scanning Calorimetry Study of Melting Transitions in Aqueous Suspensions Containing Blends of Wheat and Rice Starch”, Carbohyd Polym (1992) 17 145-149.
Liu, H., Lelievre, J., “Effects of Heating Rate and Sample Size on Differential Scanning Calorimetry Traces of Starch Gelatinized at Intermediate Water Levels”, Starch (1991) 43 225-227.
Liu, J.M. Zhao, S.L., “Scanning Electron Microscope Study on Gelatinization of Starch Granules in Excess Water”, Starch-Starke (1990) 42 96-98.
Liu, W.R., Langer, R., Klibanov, A.M., “Moisture-Induced Aggregation of Lyophilized Proteins in the Solid State”, Biotechnol Bioeng (1991) 37 177-184.
Lo, J.R., Mochizuki, Y., Nagashima, Y., Tanaka, M., Iso, N., Taguchi, T., “Thermal Transitions of Myosins Subfragments from Black Marlin (Makaira-Mazara) Ordinary and Dark Muscles”, J Food Sci (1991) 56 954-957.
Lo, J.R., Nagashima, Y., Tanaka, M., Taguchi, T., Amano, K., “Effect of Ultrasonication on the Thermal Gelation of Ordinary and Dark Meat Pastes from Yellowfin Tuna”, J Jpn Soc Food Sci Technol (1991) 38 540-544.
Lupas, A., Vandyke, M., Stock, J., “Predicting Coiled Coils from Protein Sequences”, Science (1991) 252 1162-1164.
Luthy, R., Bowie, J.U., Eisenberg, D., “Assessment of Protein Models with 3-Dimensional Profiles”, Nature (1992) 356 83-85.
Ma, C.Y., Yiu, S.H., Khanzada, G., “Rheological and Structural Properties of Wiener-Type Products Substituted with Vital Wheat Gluten”, J. Food Science (1991) 56 228-233.
Macdonald, G.A., Lelievre, J., Wilson, N.D.C., “Effect of Frozen Storage on the Gel-Forming Properties of Hoki (Macruronus-Novaezelandiae)”, J Food Sci (1992) 57 69-71.
Macdonald, G.A., Lelievre, J., Wilson, N.D.C., “Strength of Gels Prepared from Washed and
Unwashed Minces of Hoki (Macruronus-Novaezelandiae) Stored in Ice”, J. Food Science (1990) 55 976.
MacFarlane, J.J., Schmidt, G.R., Turner, R.H., “Binding of meat pieces: a comparison of myosin, actomyosin and sarcoplasmic proteins as binding agents”, J. of Food Science (1977) 42 1603-1605.
Mackey, K.L., Ofoli, R.Y., “Rheology of Low-Moisture to Intermediate-Moisture Whole Wheat Flour Doughs”, Cereal Chem (1990) 67 221-226.
Makinodan, Y. Hujita, M., “Effect of the Addition of Slivers of Ginger on the Gel Strength of Kamaboko”, Nippon Suisan Gakkaishi-Bulletin of the Japanese Society of (1990) 56 537-542.
Makinodan, Y., Hujita, M., “Textural Degradation of Cooked Fish Meat Gel (Kamaboko) by the Addition of an Edible Mushroom, Judas Ear (Auricularia-Auriculajudae (Fr) Quel)”, J. Food Science (1990) 55 979-982.
Makinodan, Y., Nakagawa, T., Hujita, M., “Effect of Addition of Powdered Ginger on Gel Strength of Kamaboko”, J Jpn Soc Food Sci Technol (1990) 37 878-883.
Mangino, M.E., “Gelation of Whey Protein Concentrates”, Food Technol (1992) 46 114.
Margoshes, B.A., “Correlation of Protein Sulfhydryls with the Strength of Heat-Formed Egg White Gels”, J. Food Science (1990) 55 1753.
Marin, M.L., Casas, C., Sanz, B., “Estimation of the Hydrophobicity Modifications in Meat Proteins upon Thermal Treatment”, J Sci Food Agr (1991) 56 187-193.
Marshall, W.E., Normand, F.L., Goynes, W.R., “Effects of Lipid and Protein Removal on Starch Gelatinization in Whole Grain Milled Rice”, Cereal Chem (1990) 67 458-463.
Martinezmendoza, A., Sherman, P., “Protein Glyceride Interaction – Influence on Emulsion Properties”, Microemulsions and Emulsions (1991) 448 130-137.
Matsudomi, N., Ishimura, Y., Kato, A., “Improvement of Gelling Properties of Ovalbumin by Heating in Dry State”, Agr Biol Chem Tokyo (1991) 55 879-881.
Matsudomi, N., Rector, D., Kinsella, J.E., “Gelation of Bovine Serum Albumin and beta-Lactoglobulin – Effects of pH, Salts and Thiol Reagents”, Food Chem (1991) 40 55-69.
Matsumoto, T., Hayashi, R., “Properties of Pressure-Induced Gels of Various Soy Protein Products”, Nippon Nogeikagaku Kaishi (1990) 64 1455-1459.
Matzke, S.F., Creagh, A.L., Haynes, C.A., Prausnitz, J.M., Blanch, H.W., “Mechanisms of Protein Solubilization in Reverse Micelles”, Biotechnol Bioeng (1992) 40 91-102.
Mayfield, T.L., Hale, K.K., Rao, V.N.M., Angulo-Chacon, I.A., “Effects of levels of fat and protein on the stability and viscosity of emulsions prepared from mechanically deboned poultry meat”, J. of Food Science (1978) 430 197-201.
Mckenna, A.B., Singh, H., “Age Gelation in UHT-Processed Reconstituted Concentrated Skim Milk”, Int J Food Sci Technol (1991) 26 27-38.
Mcmahon, D.J., Savello, P.A., Brown, R.J., Kalab, M., “Effects of Phosphate and Citrate on the Gelation Properties of Casein Micelles in Renneted Ultra-High Temperature (UHT) Sterilized Concentrated Milk”, Food Struct (1991) 10 27-36.
Means, W.J., Clarke, A.D., Sofos, J.N., Schmidt, G.R., “Binding, sensory and storage properties of algin/calcium structured beef steaks”, J. Food Science (1987) 52 252-256,262.
Meyer, J.A., Brown, W.L., Giltner, N.E., Guinn, J.R., “Effect of emulsifiers on the stability of sausage emulsions”, Food Technology (1964) 138-140.
Mine, Y., Noutomi, T., Haga, N., “Emulsifying and Structural Properties of Ovalbumin”, J Agr Food Chem (1991) 39 443-446.
Mirza, I., Lelievre, J., “Effect of Sample Dimensions and Deformation Rate on the Torsional Failure of Dumbbell Shaped Gels”, J Texture Stud (1992) 23 57-67.
Mita, T., “Effect of Aging on the Rheological Properties of Gluten Gel”, Agricultural and Biological Chemistry (1990) 54 927-935.
Mita, T., “Structure of Potato Starch Pastes in the Aging Process by the Measurement of Their Dynamic Moduli”, Carbohyd Polym (1992) 17 269-276.
Mittal, G.S., Wang, C.Y., Usborne, W.R., “Smokehouse process conditions for meat emulsion cooking”, J. Food Science (1987) 52 1140-1146,1154.
Mittal, G.S., Wang, C.Y., Usborne, W.R., “Thermal Properties of Emulsion Type Sausages During Cooking”, Canadian Institute of Food Science and Technology Journal-Jo (1989) 22 359-363.
Montejano, J.A., Hamann, D.D., Ball, H.R. Jr., Lanier, T.C., “Thermally induced gelation of native and modified egg white-rheological changes during processing; final strengths and microstrctures”, J. Food Science (1984) 49 1249-1257.
Montejano, J.G., Hamann, D.D., Lanier, T.C., “Thermally induced gelation of selected comminuted muscle systems-rheological changes during processing, final strengths and microstructure”, J. Food Science (1984) 49 1496-1505.
Montero, P., Borderias, J., “Gelification of Collagenous Material from Muscle and Skin of Hake (Merluccius-Merluccius L) and Trout (Salmo-Irideus Gibb) According to Variation in pH and the Presence of NaCl in the Medium”, Z Lebensmittel-Untersuch Fors (1990) 191 11-15.
Morris, E.R., “The Effect of Solvent Partition on the Mechanical Properties of Biphasic Biopolymer Gels – An Approximate Theoretical Treatment”, Carbohyd Polym (1992) 17 65-70.
Morrison, G.S., Webb, N.B., Blumer, T.N., Ivey, F.J., Hug, A., “Relationship between composition and stability of sausage-type emulsions”, J. of Food Science (1971) 36 426-430.
Muguruma, M., Sakamoto, K., Numata, M., Yamada, H., Nakamura, T., “Studies on Application of Transglutaminase to Meat and Meat Products .2. The Effect of Microbial Transglutaminase on Gelation of Myosin B, Myosin and Actin”, J Jpn Soc Food Sci Technol (1990) 37 446-453.
Muhrbeck, P., Eliasson, A.C., “Rheological Properties of Protein Starch Mixed Gels”, J Texture Stud (1991) 22 317-332.
Muir, D.D., Mccraehomsma, C.H., Sweetsur, A.W.M., “Characterization of Dairy Emulsions by Forward Lobe Leaser Light Scattering – Application to Cream Liqueurs”, Milchwissenschaft (1991) 46 691-694.
Mulvihill, D.M., Rector, D., Kinsella, J.E., “Mercaptoethanol, N-Ethylmaleimide, Propylene Glycol and Urea Effects on Rheological Properties of Thermally Induced beta-Lactoglobulin Gels at Alkaline pH”, J Food Sci (1991) 56 1338-1341.
Nagai, T., Nademoto, Y., Yano, T., “Improvement of Physical Properties by Increase of Specific Surface Area of Starch Gel Powder”, J Jpn Soc Food Sci Technol (1991) 38 533-539.
Nagai, T., Yano, T., “Surface Microstructure of Various Calcium Alginate Xero-Gels and Its Fractal Analysis”, J Jpn Soc Food Sci Technol (1991) 38 350-356.
Nakakura, H., Nishigaki, F., Sambuichi, M., Miura, Y., Osasa, K., “Studies on Mechanical Compression Properties of Gels”, J Jpn Soc Food Sci Technol (1992) 39 8-15.
Nakayama, T., Kimata, T., Ooi, A., “Development of Plastic Consistency in Air-Dispersed Gel”, J Jpn Soc Food Sci Technol (1992) 39 93-101.
Nakayama, T., Ooi, A., “Surface Tension, Spinnability, and Gelation of Denatured Carp Actomyosin Preparation”, Nippon Suisan Gakkaishi (1991) 57 935-942.
Naoko, Y.O., Maeda, H., Okada, M., Hasegawa, K., “Formation of Transparent Gels of Sesame 13S-Globulin – Effects of Fatty Acid Salts”, J Food Sci (1992) 57 86-90.
Nierle, W., Elbaya, A.W., Kersting, H.J., Meyer, D., “Lipids and Rheological Properties of Starch .2. The Effect of Granule Surface Material on Viscosity of Wheat Starch”, Starch (1990) 42 471-475.
Ninomiya, K., Ookawa, T., Tsuchiya, T., Matsumoto, J.J., “Concentration of Fish Water Soluble Protein and Its Gelation Properties”, Nippon Suisan Gakkaishi (1990) 56 1641-1645.
Nishimura, K., Ohtsuru, M., Nigota, K., “Mechanism of Improvement Effect of Ascorbic Acid on the Thermal Gelation of Fish Meat”, Nippon Suisan Gakkaishi (1990) 56 959-966.
Nishinari, K., Kohyama, K., Zhang, Y., Kitamura, K., Sugimoto, T., Saio, K., Kawamura, Y., “Rheological Study on the Effect of the A5-Subunit on the Gelation Characteristics of Soybean Proteins”, Agr Biol Chem Tokyo (1991) 55 351-355.
Nishinari, K. Watase, M. Williams, P.A. Phillips, G.O., “Kappa-Carrageenan Gels – Effect of Sucrose, Glucose, Urea, and Guanidine Hydrochloride on the Rheological and Thermal Properties”, Journal of Agricultural and Food Chemistry (1990) 38 1188-1193.
Nishinari, K., Williams, P.A., Phillips, G.O., “Review of the Physico-Chemical Characteristics and Properties of Konjac Mannan”, Food Hydrocolloid (1992) 6 199-222.
Nishinari, K., “Colloids, Sols and Gels”, J Jpn Soc Food Sci Technol (1990) 37 934.
Niwa, E., Chen, E., Kanoh, S., “Influence of the Fluidity of Water on the Visco-Elasticity of Food Hydrogels Examined by Using Models of a Closed System”, Agricultural and Biological Chemistry (1990) 54 393-397.
Niwa, E., Ogawa, N., Kanoh, S., “Depression of Elasticity of Kamaboko Induced by Pregelatinized Starch”, Nippon Suisan Gakkaishi (1991) 57 157-162.
Niwa, E., Ueno, S., Kanoh, S., “Mechanism for the Gelation of Unheated Surimi by Vinegar Curing”, Biosci Biotechnol Biochem (1992) 56 58-61.
Noel, Y., Durier, C., Lehembre, N., Kobilinsky, A., “Multifactorial Study of Combined
Enzymatic and Lactic Milk Coagulation Measured by Viscoelasticimetry”, Lait (1991) 71 15-39.
Notzold, H., Kretschmar, R., Ludwig, E., “Contribution to the Determination of Protein Hydrophobicity .1. Determination of the Hydrophobicity of Selected Cereal and Milk Proteins Using Their Sodium Dodecylsulphate Binding Capacities”, Nahrung (1991) 35 969-975.
Notzold, H., Kretschmar, R., Ludwig, E., “Contribution to the Determination of Protein Hydrophobicity .2. Determination of Protein-Bound Sodium Dodecylsulphate Using Ultracentrifugation Experiments”, Nahrung (1991) 35 977-980.
Nuckles, R.O., Smith, D.M., Merkel, R.A., “Properties of Heat-Induced Gels from Beef Skeletal, Heart, Lung and Spleen Protein Fractions”, J Food Sci (1991) 56 1165-1170.
Numakura, T., Kimura, I., Toyoda, K., Fujita, T., “Temperature-Dependent Changes in Gel Strength and Myosin Heavy Chain of Salt-Ground Meat from Walleye Pollack During Setting”, Nippon Suisan Gakkaishi (1990) 56 2035-2043.
Nussinovitch, A., Ak, M.M., Normand, M.D., Peleg, M., “Characterization of Gellan Gels by Uniaxial Compression, Stress Relaxation and Creep”, J TEXT STUD (1990) 21 37-49.
Nussinovitch, A., Kaletunc, G., Normand, M.D., Peleg, M., “Recoverable Work Versus Asymptotic Relaxation Modulus in Agar, Carrageenan and Gellan Gels”, J Texture Stud (1990) 21 427-438.
Nussinovitch, A., Kopelman, I.J., Mizrahi, S., “Evaluation of Force Deformation Data As Indices to Hydrocolloid Gel Strength and Perceived Texture”, Int J Food Sci Technol (1990) 25 692-698.
Nussinovitch, A., Kopelman, I.J., Mizrahi, S., “Mechanical Properties of Composite Fruit Products Based on Hydrocolloid Gel, Fruit Pulp and Sugar”, Food Sci Technol-Lebensm Wiss (1991) 24 214-217.
Nussinovitch, A., Lee, S.J., Kaletunc, G., Peleg, M., “Model for Calculating the Compressive Deformability of Double-Layered Curdlan Gels”, Biotechnol Progr (1991) 7 272-274.
Nussinovitch, A., Peleg, M., “Strength-Time Relationships of Agar and Alginate Gels”, J TEXT STUD (1990) 21 51-60.
Nyanzi, F.A., Maga, J.A., “Effect of Processing Temperature on Detergent-Solubilized Protein in Extrusion-Cooked Cornstarch Soy Protein Subunit Blends”, J Agr Food Chem (1992) 40 131-133.
Oakenfull, D., “A method for using measurements of shear modulus to estimate the size and thermodynamic stability of junction zones in noncovalently cross-linked gels”, J. Food Science (1984) 49 1103-1104,1110.
Ockerman, H.W., Wu, Y.C., “Hot-Boning, Tumbling, Salt and Chopping Temperature Effects on Cooking Yield and Acceptability of Emulsion-Type Pork Sausage”, J. Food Science (1990) 55 1255-1257.
Ogasawara, M., Nagashima, Y., Tanaka, M., Mizuno, H., Taguchi, T., “Thermal Gelation of Carbodiimide Cross-Linked Oval Filefish Myosin”, Nippon Suisan Gakkaishi (1991) 57 1789-1793.
Ogawa, N., Tanabe, H., “Effects of Salt on Rheological Properties and Scanning Electron Micrographs of Heat Induced Egg White Gels of Shell Eggs”, J Jpn Soc Food Sci Technol (1991) 38 1117-1123.
Okayama, T., Fujii, M., Yamanoue, M., “Effect of Cooking Temperature on the Percentage Colour Formation, Nitrite Decomposition and Sarcoplasmic Protein Denaturation in Processed Meat Products”, Meat Science (1991) 30 49-57.
Okechukwu, P.E., Rao, M.A., Ngoddy, P.O., Mcwatters, K.H., “Firmness of Cowpea Gels as a Function of Moisture and Oil Content, and Storage”, J Food Sci (1992) 57 91-95.
Okechukwu, P.E., Rao, M.A., Ngoddy, P.O., Mcwatters, K.H., “Flow Behavior and Gelatinization of Cowpea Flour and Starch Dispersions”, J Food Sci (1991) 56 1311-1315.
Okechukwu, P.E., Rao, M.A., Ngoddy, P.O., Mcwatters, K.H., “Rheology of Sol-Gel Thermal Transition in Cowpea Flour and Starch Slurry”, J Food Sci (1991) 56 1744-1748.
Okeefe, S.F., Resurreccion, A.P., Wilson, L.A., Murphy, P.A., “Temperature Effect on Binding of Volatile Flavor Compounds to Soy Protein in Aqueous Model Systems”, J Food Sci (1991) 56 802-806.
Olsson, A., Tornberg, E., Lee, C.M., Puolanne, E., Comer, F.W., “Fat-Holding in Hamburgers as Influenced by the Different Constituents of Beef Adipose Tissue”, Food Struct (1991) 10 333-344.
Patel, M.T., Kilara, A., Huffman, L.M., Hewitt, S.A., Houlihan, A.V., “Studies on Whey Protein Concentrates .1. Compositional and Thermal Properties”, J Dairy Sci (1990) 73 1439-1449.
Paulsson, M., Dejmek, P., Vanvliet, T., “Rheological Properties of Heat-Induced Beta-Lactoglobulin Gels”, Journal of Dairy Science (1990) 73 45-53.
Pavlova, L.A., Damshkaln, L.G., Vainerman, E.S., “Effect of Acetylation on Rheological Properties of Fish Protein Isolates During Heating”, Nahrung (1991) 35 53-59.
Penchonok, M.H., Regenstein, J.M., “Low temperature stability of emulsions made with chicken breast muscle proteins following timed emulsification”, (0) .
Pessa, E., Suortti, T., Autio, K., Poutanen, K., “Molecular Weight Characterization and Gelling Properties of Acid-Modified Maize Starches”, Starch (1992) 44 64-69.
Piculell, L., Nilsson, S., Muhrbeck, P., “Effects of Small Amounts of Kappa-Carrageenan on the Rheology of Aqueous Iota-Carrageenan”, Carbohyd Polym (1992) 18 199-208.
Pouliot, Y., Britten, M., Latreille, B., “Effect of High-Pressure Homogenization on a Sterilized Infant Formula – Microstructure and Age Gelation”, FOOD STRUCT (1990) 9 1-8.
Poullot, Y., Britten, M., Latreille, B., “Effect of high-pressure homogenization on a sterilized infant formula: microsturcture and age gelation”, Food Structure (1990) 9 1-8.
Puolanne, E.J., Terrell, R.N., “Effects of salt levels in prerigor blends and cooked sausages on water binding, released fat and ph”, J. of Food Science (1983) 48 1022-1024.
Radosta, S. Schierbaum, F., “Polymer-Water Interaction of Maltodextrins .3. Non-Freezable Water in Maltodextrin Solutions and Gels”, Starch-Starke (1990) 42 142-147.
Rector, D., Matsudomi, N., Kinsella, J.E., “Changes in Gelling Behavior of Whey Protein Isolate and beta-Lactoglobulin During Storage – Possible Mechanism(S)”, J Food Sci (1991) 56 782-788.
Rector, D.J., Kella, N.K., Kinsella, J.E., “Reversible Gelation of Whey Proteins – Melting, Thermodynamics and Viscoelastic Behavior”, Journal of Texture Studies (1990) 20 457-471.
Riva, M., Piazza, L., Schiraldi, A., “Starch Gelatinization in Pasta Cooking – Differential Flux Calorimetry Investigations”, Cereal Chem (1991) 68 622-627.
Roberts, L.H., “Sausage emulsions: functionality of non-meat proteins in perspective”.
Robin, O., Paquin, P., “Evaluation of the Particle Size of Fat Globules in a Milk Model Emulsion by Photon Correlation Spectroscopy”, J Dairy Sci (1991) 74 2440-2447.
Robins, M.M., “Effect of Polysaccharide on Flocculation and Creaming in Oil-in-Water Emulsions”, Microemulsions and Emulsions (1991) 448 230-246.
Roefs, S.P.F.M., Vanvliet, T., Vandenbijgaart, H.J.C.M., Degrootmostert, A.E.A., Walstra, P., “Structure of Casein Gels Made by Combined Acidification and Rennet Action”, Neth Milk Dairy J (1990) 44 159-188.
Rongey, E.H., “A simple objective test for sausage emulsion quality”, Proceedings of Meat Industry Reseaech Conference (1965) 99-106.
Roussel, H., Cheftel, J.C., “Mechanisms of Gelation of Sardine Proteins – Influence of Thermal Processing and of Various Additives on the Texture and Protein Solubility of Kamaboko Gels”, INT J FOOD (1990) 25 260-280.
Rutschmann, M.A., Solms, J., “Inclusion Complexes of Potato Starch – A Binding Model with Synergism and Antagonism”, Food Sci Technol-Lebensm Wiss (1991) 24 473-475.
Saeki, H., Hirata, F., Matsukawa, M., Kitanoma, K., Nonaka, M., “Studies on Development of Highly Nutritional Fish Meat for Foodstuff .8. Gel Forming Ability of Highly Nutritional Fish Meat for Foodstuff Prepared from Frozen Sardine”, Nippon Suisan Gakkaishi (1991) 57 2089-2094.
Saffle, R.L., “Meat emulsions”, Adv. Food Research (1968) 105-160.
Saffle, R.L., “1. The meat packing laboratory.–2. An objective method of determining emulsification value and color of various sausage meats.”, (?) 67-92.
Saffle, R.L., Carpenter, J.A., Moore, D.G., “Peeling ease of frankfuters I. Effects of chemical compositon, heat, collagen, and type of fat”, Food Technology (1964) 18 130-132.
Saffle, R.L., Carpenter, J.A., Moore, D.G., “Peeling ease of frankfurters II. Effects of humidity, temperature, and types and levels of corn-syrup solids”, Food Technology (1964) 18 132-134.
Saffle, R.L., Christian, J.A., Carpenter, J.A., Zirkle, S.B., “Rapid method to determine stability of sausage emulsions and effects of processing temperatures and humidities”, Food Technology (1967) 21 100-104.
Saffle, R.L., Galbreath, J.W., “Quantitative determination of salt-soluble protein in various types of meat”, Food Technology (1964) 119-129.
Saito, Y. Sato, T. Anazawa, I., “Effects of Molecular Weight Distribution of Nonionic Surfactants on Stability of O/W Emulsions”, Journal of the American Oil Chemists Society (1990) 67 145-148.
Samejima, K., Lee, N.H., Ishioroshi, M., Asghar, A., “Protein Extractability and Thermal Gel Formability of Myofibrils Isolated from Skeletal and Cardiac Muscles at Different Post-Mortem Periods”, J Sci Food Agr (1992) 58 385-393.
Sanders, E.B., Thompson, D.B., Boyer, C.D., “Thermal Behavior During Gelatinization and Amylopectin Fine Structure for Selected Maize Genotypes As Expressed in 4 Inbred Lines”, Cereal Chem (1990) 67 594-602.
Sano, T., Noguchi, S.F., Tsuchiya, T., Matsumoto, J.J., “Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation”, J. Food Science (1988) 53 924-928.
Sase, H., Watanabe, M., Arai, S., Ogawa, Y., “Functional and sensory properties of meat emulsions produced by using enzymatically modified gelatin”, J. Food Science (1987) 52 893-895,900.
Schmandke, H., Schultz, M., Schmidt, G., Schneider, C., Andersson, O., “Tension of Oil-Water Interface and Properties of O/W Emulsions in Dependence of Faba Bean Globulins”, Nahrung (1990) 34 363-368.
Schmidt, G.R., Trout, G.R., “The chemistry of meat binding”, Recent Advances in the Chemistry of Meat (0) 231-243.
Schmidt, R.H., Morris, H.A., “Gelation properties of milk proteins, soy proteins, and blended protein systems”, Food Technology (1984) 85-96.
Shoji, T., Saeki, H., Wakameda, A., Nakamura, M., Nonaka, M., “Gelation of Salted Paste of Alaska Pollack by High Hydrostatic Pressure and Change in Myofibrillar Protein in It”, Nippon Suisan Gakkaishi (1990) 56 2069-2076.
Sievert, D., Sapirstein, H.D., Bushuk, W., “Changes in Electrophoretic Patterns of Acetic Acid-Insoluble Wheat Flour Proteins During Dough Mixing”, J Cereal Sci (1991) 14 243-256.
Smith, D.M., Alvarez, V.B., Morgan, R.G., “A generalized model for predicting heat-induced chicken myofibrillar protein gel strength”, J. Food Science (1988) 53 359-362.
Smith, D.M., “Factors Influencing Heat-Induced Gelation of Muscle Proteins”, Interactions of Food Proteins (1991) 454 243-256.
Sochava, I.V., Belopolskaya, T.V., “Thermally Induced Globular Protein Gels – Peculiarities of Formation, Melting, and Restoration of Gels of Different Structure”, Food Hydrocolloid (1992) 6 97-114.
Stading, M., Hermansson, A.M., “Large Deformation Properties of beta-Lactoglobulin Gel Structures”, Food Hydrocolloid (1991) 5 339-352.
Stampanoni, C.R., Noble, A.C., “The Influence of Fat, Acid, and Salt on the Temporal Perception of Firmness, Saltiness, and Sourness of Cheese Analogs”, J Texture Stud (1991) 22 381-392.
Steventon, A.J., Gladden, L.F., Fryer, P.J., “A Percolation Analysis of the Concentration Dependence of the Gelation of Whey Protein Concentrates”, J Texture Stud (1991) 22 201-218.
Susheelamma, N.S., Chand, N., Rajalakshmi, D., “Modelling the Gelling Behaviour of Linseed Polysaccharide”, J Texture Stud (1991) 22 413-421.
Suzuki, A., Kaneyama, M., Shibanuma, K., Takeda, Y., Abe, J., Hizukuri, S., “Characterization of Lotus Starch”, Cereal Chem (1992) 69 309-315.
Suzuki, A., Tanaka, T., “Phase Transition in Polymer Gels Induced by Visible Light”, Nature (1990) 346 345-347.
Suzuki, K., Maeda, T., Matsuoka, K., Kubota, K., “Effects of Constituent Concentration on Rheological Properties of Corn Oil-in-Water Emulsions”, J Food Sci (1991) 56 796.
Svegmark, K., Hermansson, A.M., “Changes Induced by Shear and Gel Formation in the Viscoelastic Behaviour of Potato, Wheat and Maize Starch Dispersions”, Carbohyd Polym (1991) 15 151-169.
Swatland, H.J., “A Note on the Growth of Connective Tissues Binding Turkey Muscle Fibers Together”, Can Inst Food Sci Technol J (1990) 23 239-241.
Swift, C.E., Lockett, C., Fryar, A.J., “Comminuted meat emulsions-the capacity of meats for emulsifying fat”, Food Technology (1961) 468-473.
Takahashi, J., Nakazawa, F., “Palatal Pressure Patterns of Gelatin Gels in the Mouth”, J Texture Stud (1991) 22 1-11.
Tako, M., Kiriaki, M., “Rheological Properties of Welan Gum in Aqueous Media”, Agr Biol Chem Tokyo (1990) 54 3079-3084.
Tako, M., Sakae, A., Nakamura, S., “Rheological properties of gellan gum in aqueous media”, Agric. Biol. Chem. (1988) 53 771-776.
Tamime, A.Y., Kalab, M., Davies, G., Mahdi, H.A., “Microstructure and Firmness of Labneh (High Solids Yoghurt) Made from Cow’s, Goat’s and Sheep’s Milks by a Traditional Method or by Ultrafiltration”, Food Struct (1991) 10 37-44.
Tamime, A.Y., Kalab, M., Davies, G., Martin, R.W., Goff, H.D., Olsen, R., “The Effect of Processing Temperatures on the Microstructure and Firmness of Labneh Made from Cows Milk by the Traditional Method or by Ultrafiltration”, Food Struct (1991) 10 345-352.
Tanaka, H., Nonaka, M., Motoki, M., “Polymerization and Gelation of Carp Myosin by Microbial Transglutaminase”, Nippon Suisan Gakkaishi (1990) 56 1341.
Tester, R.F., Morrison, W.R., “Swelling and Gelatinization of Cereal Starches .1. Effects of Amylopectin, Amylose, and Lipids”, Cereal Chem (1990) 67 551-557.
Tester, R.F., Morrison, W.R., “Swelling and Gelatinization of Cereal Starches .2. Waxy Rice Starches”, Cereal Chem (1990) 67 558-563.
Thompson, L.D., Janky, D.M., Arafa, A.S., “Emulsion and storage stabilities of emulsions incorporating mechanically deboned poultry meat and various soy flours”, J. Food Science (1984) 49 1358-1362.
Toyohara, H., Kinoshita, M., Sasaki, K., Shimizu, Y., “Change of the Myofibril-Associated Type of the Modori-Phenomenon After Death”, Nippon Suisan Gakkaishi (1990) 56 1251-1253.
Toyohara, H. Sakata, T. Yamashita, K. Kinoshita, M. Shimizu, Y., “Degradation of Oval-Filefish Meat Gel Caused by Myofibrillar Proteinase(S)”, Journal of Food Science (1990) 55 364-368.
Toyohara, H., Sasaki, K., Kinoshita, M., Shimizu, Y., Sakaguchi, M., “Detection of Inhibitors for Modori-Inducing Proteinase in Fish and Calf Serums”, Nippon Suisan Gakkaishi (1991) 57 521-525.
Toyohara, H., Sasaki, K., Kinoshita, M., Shimizu, Y., “Effect of Bleeding on the Modori-Phenomenon and Possible Existence of Some Modori-Inhibitor(S) in Serum”, Nippon Suisan Gakkaishi (1990) 56 1245-1249.
Tran, K.M., Einerson, M.A., “A rapid method for the evaluation of emulsion of non-dairy creamers”, J. Food Science (1987) 52 1109-1110.
Trout, G.R., Schmidt, G.R., “Effect of phosphate type and concentration, salt level and method of preparation on binding in restructured beef rolls”, J. Food Science (1984) 49 687-694.
Trout, G.R., Schmidt, G.R., “Water binding ability of meat products: effect of fat level, effective salt concentration and cooking temperature”, J. Food Science (1986) 51 1061-1062.
Tsai, T.C., Ockerman, H.W., “Water binding measurement of meat”, J. of Food Science (1981) 46 697-701,707.
Tsukamasa, Y., Shimizu, Y., “Another Type of Proteinase-Independent Modori (Thermal Gel Degradation) Phenomenon Found in Sardine Meat”, Nippon Suisan Gakkaishi (1991) 57 1767-1771.
Uram, G., Carpenter, J.A., Reagan, J.O., “Effects of particle size, casing diameter, and addition of emulsions and residual nitrite on quality attributes of cooked salami”, J. of Food Science (1981) 46 842-844.
Uram, G.A., Carpenter, J.A., Reagan, J.O., “Effects of emulsions, particle size and levels of added water on the acceptability of smoked sausage”, J. Food Science (1984) 49 966-967.
Ustunol, Z., Xiong, Y.L.L., Means, W.J., Decker, E.A., “Forces Involved in Mixed Pork Myofibrillar Protein and Calcium Alginate Gels”, J Agr Food Chem (1992) 40 577-580.
Vadehra, D.V., Baker, R.C., “The mechanism of heat initiated binding of poultry meat”, Food Technology (1970) 24 42-55.
Wang, C.H., Damodaran, S., “Thermal Destruction of Cysteine and Cystine Residues of Soy Protein Under Conditions of Gelation”, J. Food Science (1990) 55 1077-1080.
Wang, C.H., Damodaran, S., “Thermal Gelation of Globular Proteins – Influence of Protein Conformation on Gel Strength”, J Agr Food Chem (1991) 39 433-438.
Wang, C.H. Damodaran, S., “Thermal Gelation of Globular Proteins – Weight-Average Molecular Weight Dependence of Gel Strength”, Journal of Agricultural and Food Chemistry (1990) 38 1157-1164.
Wang, C.R., Zayas, J.F., “Emulsifying Capacity and Emulsion Stability of Soy Proteins Compared with Corn Germ Protein Flour”, J Food Sci (1992) 57 726-731.
Wang, C.R., Zayas, J.F., “Water Retention and Solubility of Soy Proteins and Corn Germ Proteins in a Model System”, J Food Sci (1991) 56 455-458.
Wang, S.F., Smith, D.M., Steffe, J.F., “Effect of pH on the Dynamic Rheological Properties of Chicken Breast Salt-Soluble Proteins During Heat-Induced Gelation”, Poultry Sci (1990) 69 2220-2227.
Watanabe, M., Kumeno, K., Nakahama, N., Arai, S., “Heat-Induced Gel Properties of Freeze-Concentrated Egg White Produced Using Bacterial Ice Nuclei”, Agr Biol Chem Tokyo (1990) 54 2055-2059.
Watase, M. Nishinari, K. Williams, P.A. Phillips, G.O., “Agarose Gels – Effect of Sucrose, Glucose, Urea, and Guanidine Hydrochloride on the Rheological and Thermal Properties”, Journal of Agricultural and Food Chemistry (1990) 38 1181-1187.
Weinberg, Z.G., Regenstein, J.M., Baker, R.C., “Effects of salt on heat initiated binding and water retention properties of comminuted cod muscle”.
Wendakoon, C.N., Shimizu, Y., Yada, T., “Effect of Starvation and Diet on the Gel Forming Ability of Tilapia (Oreochromis-Niloticus)”, J Sci Food Agr (1991) 54 295-304.
Westerbeek, J.M.M., Prins, A., “Function of alpha-Tending Emulsifiers and Proteins in Whippable Emulsions”, Microemulsions and Emulsions (1991) 448 146-160.
White, D.C., Lauer, G.N., “Predicting Gelatinization Temperatures of Starch Sweetener Systems for Cake Formulation by Differential Scanning Calorimetry .1. Development of a Model”, Cereal Food World (1990) 35 728.
Whiting, R.C., “Influence of lipid composition on the water and fat exudation and gel strength of meat batters”, J. Food Science (1987) 52 1126-1129.
Whiting, R.C., “Influence of various salts and water soluble compounds on the water and fat exudation and gel strength of meat batters”, J. Food Science (1987) 52 1130-1132,1158.
Whiting, R.C., “Stability and gel strength of frankfurter batters made with reduced naci”, J. Food Science (1984) 49 1350-1354,1362.
Wolters, M.G.E., Cone, J.W., “Prediction of Degradability of Starch by Gelatinization Enthalpy as Measured by Differential Scanning Calorimetry”, Starch (1992) 44 14-18.
Woodward, S.A., “Egg Protein Gels”, Food Gels (1990) 175-199.
Wu, J.Q., Hamann, D.D., Foegeding, E.A., “Myosin Gelation Kinetic Study Based on Rheological Measurements”, J Agr Food Chem (1991) 39 229-236.
Wu, M.C., Lanier, T.C., Hamann, D.D., “Rigidity and viscosity changes of croaker actomyosin during thermal gelation”, J. Food Science (1985) 50 14-19,25.
Wu, Y.J., Atallah, M.T., Hultin, H.O., “The Proteins of Washed, Minced Fish Muscle Have Significant Solubility in Water”, J Food Biochem (1991) 15 209-218.
Xiong, Y.L., Brekke, C.J., “Physicochemical and Gelation Properties of Prerigor and Postrigor Chicken Salt-Soluble Proteins”, J. Food Science (1990) 55 1544-1548.
Xiong, Y.L., Brekke, C.J., “Protein Extractability and Thermally Induced Gelation Properties of Myofibrils Isolated from Prerigor and Postrigor Chicken Muscles”, J. Food Science (1991) 56 210-215.
Xiong, Y.L., Brekke, C.J., “Thermal Transitions of Salt-Soluble Proteins from Prerigor and Postrigor Chicken Muscles”, J. Food Science (1990) 55 1540.
Xiong, Y.L., Kinsella, J.E., “Influence of Fat Globule Membrane Composition and Fat Type on the Rheological Properties of Milk Based Composite Gels .1. Methodology”, Milchwissenschaft (1991) 46 150-152.
Xiong, Y.L., Kinsella, J.E., “Influence of Fat Globule Membrane Composition and Fat Type on the Rheological Properties of Milk Based Composite Gels .2. Results”, Milchwissenschaft (1991) 46 207-212.
Xiong, Y.L., Kinsella, J.E., “Mechanism of Urea-Induced Whey Protein Gelation”, J Agr Food Chem (1990) 38 1887-1891.
Xiong, Y.L.L., “Influence of pH and Ionic Environment on Thermal Aggregation of Whey Proteins”, J Agr Food Chem (1992) 40 380-384.
Xiong, Y.L.L., “Thermally Induced Interactions and Gelation of Combined Myofibrillar Protein from White and Red Broiler Muscles”, J Food Sci (1992) 57 581-585.
Xu, S.Y., Stanley, D.W., Goff, H.D., Davidson, V.J., Lemaguer, M., “Hydrocolloid Milk Gel Formation and Properties”, J Food Sci (1992) 57 96-102.
Yamamoto, K., Miura, T., Yasui, T., “Gelation of Myosin Filament Under High Hydrostatic Pressure”, Food Struct (1990) 9 269-277.
Yamazawa, M., “Studies on the Mechanism of Gel-Reinforcing Effect of Starch in Kamaboko-Gel .1. Effect of Heating Temperature on Structure and Gel-Reinforcing Ability of Starch Granules in Kamaboko-Gel”, Nippon Suisan Gakkaishi (1990) 56 505-510.
Yamazawa, M., “Studies on the Mechanism of Gel-Reinforcing Effect of Starch in Kamaboko-Gel .2. Relationship Between the Water-Absorbing Ability of Starch Granules and Their Kamaboko-Gel Reinforcing Effect”, Nippon Suisan Gakkaishi (1991) 57 965-970.
Yamazawa, M., “Studies on the Mechanism of Gel-Reinforcing Effect of Starch in Kamaboko-Gel .3. Relationship Between the Swelling Ability of Starch Granules and Their Kamaboko-Gel Reinforcing Effect”, Nippon Suisan Gakkaishi (1991) 57 971-975.
Yano, T., “Kinetic Study on Gelation of Fish Meat Sol”, Journal of the Japanese Society for Food Science and Technol (1990) 37 220-223.
Yao, J.J., Tanteeratarm, K., Wei, L.S., “Effects of Maturation and Storage on Solubility,
Emulsion Stability and Gelation Properties of Isolated Soy Proteins”, J Amer Oil Chem Soc (1990) 67 974-979.
Yasui, T., Samejima, K., “Recent Advances in Meat Science in Japan – Functionality of Muscle Proteins in Gelation Mechanism of Structured Meat Products”, JARQ-Jpn Agr Res Quart (1990) 24131-140.
Yazawa, T., Mizuno, H., Ogawa, H., Yamada, K., Matsuno, S., Saito, T., Iso, N., “Volume Change Accompanied with Sol-Gel Transition of Fish Meat Sol”, Nippon Suisan Gakkaishi (1991) 57 915-917.
Yetim, H., Gokalp, H.Y., Kaya, M., Yanar, M., Ockerman, H.W., “Physical, Chemical and
Organoleptic Characteristics of Turkish Style Frankfurters Made with an Emulsion Containing Turkish Soy Flour”, Meat Sci (1992) 31 43-56.
Yilmazer, G., Carrillo, A.R., Kokini, J.L., “Effect of Propylene Glycol Alginate and Xanthan Gum on Stability of o/w Emulsions”, J Food Sci (1991) 56 513-517.
Yilmazer, G., Kokini, J.L., “Effect of Polysorbate-60 on the Stability of O/W Emulsions
Stabilized by Propylene Glycol Alginate and Xanthan Gum”, J Texture Stud (1991) 22 289-301.
Yoon, K.S., Lee, C.M., Hufnagel, L.A., “Textural and Microstructural Properties of Frozen Fish Mince as Affected by the Addition of Nonfish Proteins and Sorbitol”, Food Struct (1991) 10 255-265.
Yoon, K.S., Lee, C.M., “Cryoprotectant Effects in Surimi and Surimi Mince-Based Extruded Products”, J. Food Science (1990) 55 1210-1216.
Yoshida, M., Kohyama, K., Nishinari, K., “Gelation Properties of Soymilk and Soybean 11S Globulin from Japanese-Grown Soybeans”, Biosci Biotechnol Biochem (1992) 56 725-728.
Yu, M.A., Damodaran, S., “Kinetics of Protein Foam Destabilization – Evaluation of a Method Using Bovine Serum Albumin”, J Agr Food Chem (1991) 39 1555-1562.
Zanoni, B., Smaldone, D., Schiraldi, A., “Starch Gelatinization in Chemically Leavened Bread Baking”, J Food Sci (1991) 56 1702.
Zheng, B.A., Matsumura, Y., Mori, T., “Thermal Gelation Mechanism of Legumin from Broad Beans”, J Food Sci (1991) 56 722-725.
Ziegler, G.R., Acton, J.C., “Mechanisms of gel formation by proteins of muscle tissue”, Food Technology (1984) 77-82.
Ziegler, G.R., “Microstructure of Mixed Gelatin-Egg White Gels – Impact on Rheology and Application to Microparticulation”, Biotechnol Progr (1991) 7 283-287.