Proteins: choosing the right application

Consumer demand for more natural ingredients is increasing. Whey and soy are the leading sources of protein for foods, and the range of oilseed sources is offering product developers even more alternatives. Researchers at The Netherlands' Wageningen University and Research Centre discuss alternatives and variables to keep in mind

Proteins are being used as ingredients in man-made food products because they contribute to one or more of the desired characteristics of that food product. These characteristics might be consumer related, such as texture, mouthfeel, appearance or taste, as well as technology related. The latter includes both storage — shelf life and palatability — and processing, such as mixing behaviour, foam, emulsion or gel formation. Proteins contribute to one or more of these characteristics because of their functional properties — physicochemical properties that govern the performance and behaviour of a protein in food systems during preparation, processing, storage and consumption.1

It is the exact composition, spatial structure and size that determine how proteins 'act' in food products, thus how they function. Extrinsic factors such as pH and temperature; the presence of other constituents, such as salts, surfactants, gums, water and more; and process treatments all can alter the performance. Therefore, the functionality of a protein is largely affected by circumstances. The behaviour in model systems can be different from that in real food products. There are many reasons for these discrepancies.

  • The interactions of the proteins with other components in the food product.
  • The use of water by other components, so less water is available for the protein.
  • Usually mixtures of proteins are being used. Most industrial protein preparations derived from a particular source, such as soy, egg or milk, are mixtures of different types. Furthermore, in food different protein sources are often intentionally mixed, mostly for nutritious or economic reasons.2
  • The purification or isolation process used may have irreversibly affected the behaviour of the protein.
  • The structure of the food may cause local differences in composition.
  • The exact treatment during processing may be inhomogeneous; an example of this is the effect of product size on the local temperature during heating.

Furthermore, the use of a protein in a product is governed by, on one hand, economic considerations — costs of preparation and handling, availability, and constancy in quality, for example — and on the other hand, by technological ones. Regarding the latter, the protein should contribute as much as possible to the optimal combination of functional properties required to reach the full palette of desired product characteristics. For example, egg white, a rather expensive protein preparation, is used in meringues primarily because of its excellent foaming properties. However, its good gelling properties are also of major importance for this application. The combination of functional properties should be optimal; each separate functionality need not be maximal.

Protein-flavour relationships
In addition to the effects of proteins on the texture and the mouthfeel of food products, the complex conformational structure of proteins creates an important source for interactions with flavour compounds influencing the flavour perception of food products. In general, proteins themselves have little flavour of their own. However, the complex conformational structure of proteins creates an important source for (ir)reversible interactions with flavour compounds. This ability is exploited in several ways, both with respect to enhancing and masking the flavour of food products. Flavour compounds are often deliberately added to food to enhance its smell and taste. Proteins may then serve to bind these compounds, in other words to act as a reservoir.

In this context another application of proteins can be mentioned. Proteins, for example as gelatin, are used to encapsulate flavour compounds to protect them from deterioration during processing. The latter usage may even result in controlled release of flavour compounds, for instance during chewing.3

In general, the internal region of a protein, being rather hydrophobic, is able to bind nonpolar flavour compounds, while the hydrophilic surface of the protein enables interactions with polar compounds. Small increases in the protein content can significantly decrease the perception of certain flavour compounds, 4 and therefore change the sensory properties of a given food to a large extent. Two prime examples that demonstrate the importance of flavour-protein interaction are whey and soy proteins.

Whey proteins are a byproduct of the cheese industry, generated in large amounts. They are added to food systems because of their good rheological and surfactant functionalities. Another important reason for the use of whey proteins is their ability to form fatlike systems. In this way protein-based fat substitutes are used to simulate the mouthfeel of fat. Whey proteins are able to bind various types of compounds. Specifically, beta-lactoglobulin is known for its interaction with a large variety of hydrophobic ligands.5,6,7 This protein has been used by several research groups as a model macromolecule for flavour release measurements.8,9 It was found that the release of flavour depended on protein concentration. Also, these researchers showed that flavour compounds within the same chemical class had an increase in binding affinity with an increase in chain length. This effect was also observed for a homologous series of ethyl esters in the aqueous phase of sodium caseinate.10

During the production and storage of whey protein concentrate (WPC) the formation of an off-flavour is possible. Among others, lipid oxidation may result in formation of short-chain aldehydes that have a high affinity for long-term binding by covalent interactions with whey proteins. Flavour formation is of special importance when whey proteins are stored at a high water activity, resulting in an increase in the formation of aldehydes, ketones, furans and sulphur-containing compounds.5 The strongest binding affinities were observed for WPC, while the separate proteins alpha-lactalbumin and beta-lactoglobulin did not contribute that much to the flavour-binding capacity of the total whey protein, due to their low binding affinities.11

In food product development the different effects mentioned above are mostly used to reduce negative sensory attributes. A common example is the usage in coffee whiteners. Sodium caseinate is often used in these products. The actual content in the recipe varies depending on the fat content because in low-fat products it is also used as a fat replacer. Due to the high content of fat or protein, these coffee additives change completely the perception of the coffee beverage. 12

Soy proteins from soybeans provide a high-quality protein, but the demand for this protein is hampered because soy protein preparations are often associated with an undesirable flavour.13 In contrast to alcohols, which do not interact with soy protein, aldehydes, especially unstaturated aldehydes, react with the protein.14 This reaction is at least partly irreversible. The binding constant increases with the chain length by three orders of magnitude.15 Specifically, the medium-chain aldehydes largely contribute to the 'beany' and 'grassy' off-flavour of soy protein.16

Aqueous solution of soy protein isolates showed in their headspace besides the aldehydes also sulphur-containing odour active compounds like dimethyl trisulfide. Also, these constituents contribute to the well-known unpleasant odour of this protein.17

Because the soy-protein fractions 11S and 7S showed different binding affinities, with a different temperature dependency, it is possible to remove certain off-flavours by reversibly altering the quaternary structure.18 This process could be exploited for soy

protein, food processing and the formulation of soy-protein flavourings. Knowledge of the exact interactions and binding processes allows food technologists to increase the usage possibilities for soy proteins. In food processing, the different flavour binding abilities are also important for the right choice of encapsulation material. Researchers showed that soy protein isolate was most effective while whey protein isolate was least effective for retaining orange oils during spray-drying of the liquid orange-oil emulsions. 19,20
For more information on formulating for beverages, see 'Formulations.'
In the future, novel and functional foods will play important roles in our daily lives. Therefore, ingredients with new sensory attributes and/or improved nutritional value will be introduced to the market. For example, proteins such as thaumatin, monellin and miraculin have an exceptional position because of their sweet taste attributes. Traditionally, they have been used by West Africans for flavour improvement and bitterness suppression. Because consumer demand for more natural ingredients is increasing, taste-modifying proteins might be an alternative as long as they have similar properties to food products. 21

Furthermore, certain protein preparations could be used not only for optimizing sensoric properties but also the nutritional value of food products.22 Researchers showed that whey powder that was used to replace milk powder in yoghurt was preferred by sensory panelists. In addition to this preference whey powder is an important source for lactose, calcium and soluble vitamins — the nutritional value of this food product was increased.

Proteins from oil-producing plants
With a few exceptions, oil-producing plants have not generally been regarded as prime sources of protein for human consumption. Yet many of the oil-producing plants contain an appreciable level of protein, which has great potential for use in the human diet. Included in this group of oil-producing plants are soybean, canola (rapeseed), sunflower, safflower, peanut, corn, cottonseed, sesame, flax and even hemp.

The levels of protein in these seeds range from 13-17 per cent for safflower,23,24 to as high as 37 per cent for soybean.25 Despite these differences in protein levels, there are many similarities between these oilseed proteins. These proteins have similar molecular weights, subunits, amino-acid profiles and secondary structure.26 This has resulted in similar hydrophobicity values and similar association-dissociation behaviour in response to pH. These oilseed proteins, however, exhibit distinct differences in terms of tertiary structure and surface properties.26

A unique characteristic of canola protein, for instance, is the isoelectric point, which is around pH 7,27 compared to pH 4.5 to pH 5 as is the case for other oilseed proteins.23 The effect of this difference can be seen in the protein solubility where minimal solubility has been reported at both pH 4.0 and pH 8.0 compared to a single minimum around pH 4.5 for other oilseed proteins.

The range of food products that can potentially include proteins from oil-producing plants is extensive. However, with respect to proteins for oil-producing plants, the term 'potential' is significant in that demonstrated uses are primarily at an experimental level and these proteins have yet to receive that commercial recognition seen by soy protein. Nevertheless, for these proteins to become commercially viable, these experimental applications must be researched. Baked goods comprise one area where protein isolates can be used to improve nutritional quality. Adding 18 per cent sesame protein isolate to bread was possible without significantly altering the sensory properties.28 With succinylated sesame proteins, the maximum level of addition was only 10 per cent and required changes to the bread preparation protocol.29 Peanut proteins, as components in peanut flour, have also been incorporated into baked goods as well as a variety of other products.30 Sunflower protein was included in an extruded product where 10-20 per cent protein isolate was included with corn starch.31

Other possible uses for these proteins that have been reported include incorporation of peanut protein into cheese,32 use of flax proteins as additives in ice cream and fish sauce,33 use of sunflower protein hydrolysates in high-energy beverages,34 and the use of corn protein that had been treated with citric acid to increase metal-binding capacity use as a scavenger in waste-water treatments.35

The use of these proteins and products associated with these proteins may also find a place in the nutraceutical/functional-food arena. Peptides from the hydrolysis of these proteins may be bioactive and have a role in disease prevention. Minor components such as phytic acid and phenolic compounds, which have been considered antinutritional and detrimental to protein functionality, may be recovered for use in this area, as both have been shown to have properties that may have health benefits.36

As the production of oilseed will continue to supply the demand for food-grade oil, there will be a great deal of protein available from the oilseeds. While more research is required, there will be a place for these proteins in both food and nonfood applications.

(Excerpted from Proteins?in Food Processing, RY Yada, editor. ISBN 0-8493-2536-6, Published by Woodhead Publishing Ltd, England.

Dr H Luyten, Dr J Vereijken and Dr M Buecking are at Wageningen University and Research Centre, Agrotechnology &; Food Innovations, The Netherlands.

Respond: [email protected]

Which foods are the best sources of protein?
The paradox of the vegetarian diet
Studies have shown that vegetarians consume more nutritious diets than nonvegetarians. They are generally healthier, with lower cholesterol and blood pressure, and decreased rates of hypertension, diabetes and some cancers. In addition, vegetarians have lower body mass indexes (BMIs) than nonvegetarians. However, to get the daily recommended protein intake, vegetarians may need to consume more calories than nonvegetarians.

Methods: We determined how many calories were in 28grams of protein from various foods that vegetarians and nonvegetarians typically consume. This is the amount that is a typical serving of protein at a meal. We used the United States Department of Agriculture Nutrient Data Laboratory to find calorie and protein contents of these foods. Other foods were evaluated but not included.

Results: 28 grams of protein had more calories in the vegetarian foods than nonvegetarian foods. Protein (28g) from meat and dairy sources averaged 264—53 calories and 376—151 calories, respectively. However, 28 grams of protein from vegetarian sources had caloric averages of 406—74 for legumes, 737—141 for seeds and nuts, and 869—203 for grains.

Based on this selection of foods, vegetarians consumed about 66 per cent (about 500kcal) more calories than nonvegetarians to get the same amount of protein. If we assume that 3,500kcal equals one pound of body weight, then the expected weight gain could be 50 pounds during a year for someone following a vegetarian diet. This is likely an underestimate of the potential weight gain because 28 grams is less than one half the required daily protein needs.

Conclusion: A paradox exists in that vegetarians typically weigh less than nonvegetarians, yet, according to our calculations, vegetarians appear to need to consume more calories to achieve their required protein needs. To explain this conundrum, it is likely that vegetarians have adopted other healthy eating practices so that they consume mostly energy-dense foods and avoid those foods rich in sugars and fats. This way, they can afford to consume greater calories associated with their protein intake.

(See 'Protein Sources' chart below.)

Wendy Van Ausdal and Stacey J Bell are researchers at IdeaSphere, which produces nutrition products, including tablets, capsules, powder drink mixes, nutritional snacks and bars.


Amount needed to supply 28g protein


Chicken (cooked)*

4oz (113.4g)


Soy milk (2%)

2.6 cups


Whey protein isolate




1 cup


Split peas

1.7 cups


Brown rice

6 cups


Whole hempseed



*Representative of other meats and seafood

Powdered protein a texturizing challenge
Adding protein to carbohydrate-containing sports beverages provides superior benefits to beverages based on carbohydrates alone by enhancing the efficiency of carbohydrate utilisation, improving muscle-tissue repair and reducing muscle-fibre damage. However, the wide variety of powdered-protein products and their different performances in liquids pose a real challenge for anyone involved in sports-drink manufacture.

Whey protein concentrate and whey protein isolate are the most common sources of proteins used in sports nutrition worldwide. These powders typically contain protein levels of between 60 per cent and 90 per cent, a concentration that strongly influences their reconstitution characteristics.

The higher the protein level, the more hydrophilic the powder becomes and the more challenging the behaviour of the powder during reconstitution. A gelatinous layer forms at the interface of the powder and water and this barrier prevents the water from penetrating the powder particles.

Consequently, the powder does not disperse but remains on the surface of the liquid and lumps during stirring.

Technologies for instantisation
Manufacturers of protein-powder products typically use different technologies to facilitate reconstitution with instantised whey-protein powders. Two technologies in particular are used:

  • Agglomeration, resulting in an increased particle size and more porous powder structure, which improves the penetration of the liquid
  • Use of a surface-active agent, which compensates for the inconvenient powder surface behaviour

Lecithins are nature's principal emulsifying agents; in the dairy industry lecithin has for decades been the traditional emulsifier used for instantising whole-milk powder. There are many different types of lecithin, but the active components they all have in common are phospholipids.

These consist of hydrophobic long-chain fatty acids counterbalanced with polar, hydrophilic phosphates. A concentration of phospholipids at the oil/water interface lowers the surface tension and makes it possible for emulsions to form. Once this occurs, the phospholipids at the surface of the oil or water droplets form barriers to prevent the droplets from coalescing.

Due to the fact that lecithin is typically applied to the powder at the latest stage of instantization processes with no additional downstream preservation stage, the lecithin used should fulfil the highest quality standards.

Ilona Stoffels is EMEA Application Expert, Convenience &; Confectionery, Cargill Texturizing Solutions. Its Metarin EWD NGM is an enzymatically hydrolysed, liquid soybean lecithin of guaranteed non-GM origin for use with highly concentrated protein products. It improves the wettability and dispersibility of powdered protein in products in liquid, resulting in a fast and effective instantization of the protein powder.

Mini directory
American Casein Company
Manufactures caseinates, caseins, micellar casein, hydrolyzed proteins, milk protein concentrates and isolates.

Arla Foods
Northern Europe's largest dairy manufacturers of milk, cheese, yoghurt, cream and other dairy products; has a whey-protein product, Lacprodan Alpha-10, which is used in infant milk formula.

Cargill Texurizing Solutions
Offers specific solutions for providing texture in multiple food and beverage applications, based on a wide palette of ingredeints including hydrocolloids, lecithin, cultures, starches, soy flour and functional systems.

Davisco Foods International
Minnesota whey-protein manufacturer offers an instantized whey-protein concentrate.

Produces Benesoy line of ingredients, including liquid soy proteins, soy protein powders and soy flours. All are available organic. Soy flours are made from non-GMO whole soybeans.

DMV International
Producer and marketer of milk, whey and protein-based ingredients including soy-, dairy-whey/casein-based proteins including soy, whey, wheat and casein hydrolysates and milk proteins . Also offers speciality proteins and peptides such as lactoferrin and bioactive peptides.

DSM Food Specialties
PeptoPro protein hydrolysate delivers protein in the form of peptides for muscle recovery, and is used primarily in sports-recovery drinks.

Glanbia Nutritionals
Irish company's citrus-flavoured recovery drink Provon Revive has been named official recovery drink for the Leinster rugby team. Prolibra is a whey protein-derived milk mineral complex specifically for weight-management applications. Thermax690 is a heat-stable whey-protein isolate for RTD beverages. Also offers a range of whey-protein isolates, concentrates and fractions.

Hilmar Ingredients
California-based manufacturer of whey-protein isolates, hydrolysates and concentrates, aimed in particular at sports-beverage marketers and manufacturers.

Kerry Ingredients
Irish ingredients giant offers milk proteins, texture proteins, soy proteins and Hyprol vegetable protein hydrolysates.

NutraGammax is rich in bioactive proteins, which help promote amino-acid utilisation. The proteins are more complex in structure than whey or casein with a slow rate of digestion, allowing them to retain biological activity. Ideally, NutraGammax should be combined with whey or other protein sources lower in molecular weight with a more rapid rate of digestion.

Nutralys pea protein has a good amino-acid profile and works well in combination with other proteins.

Solae holds more than 100 US patents; its branded soy proteins include Alpha, Danpro, Samprosoy, Centrolex, Promine, Procote, Supro and Proplus. Solae acquired Cargill's Prolisse isolated soy-protein line earlier this year.

Stauber Performance Ingredients
Company offers soy, casein and whey-protein concentrates. It is the marketing respresentative for Proliant's Nutra Gammax.

Canadian concern has an extensive background in ion-exchange, drying and filtration technologies for the whey-protein market.

1. Kinsella JE, Whitehead DM. Proteins in whey: chemical, physical and functional properties. In Kinsella JE, Advances in food and nutrition research. Academic Press 1989:343-438.
2. Comfort S, Howell NK. Gelation properties of soy and whey protein isolate mixtures. Food hydrocolloids 2002;16:661-72.
3. Taylor AJ, Lonford RST. Flavour release in the mouth. Trends Food Sci Tech 1996;7(12):444-8.
4. Hansen AP, Heinis JJ. Decrease of vanillin flavour perception in the presence of casein and whey proteins. J Dairy Sci 1991;75:2936-40.
5. Lee YB, et al. Formation of volatile compounds in whey protein concentrate during elevated temperature storage as a function of water activity. Int Dairy J 1996;6:485-96.
6. De Wolf FA, Brett GM. Ligand-binding proteins: their potential for application in systems for controlled delivery and uptake of ligands. Pharmacol Rev 2000;52:207-36.
7. Muresan S, et al. Interaction of beta-lactoglobulin with small hydrophobic ligands as monitored by fluorimetry and equilibrium dialysis — nonlinear quenching effects related to protein-protein association. J Agr Food Chem 2001;52:2609-18.
8. Guichard E, Langourieux S. Interactions between beta-lactoblobulin and flavour compounds. Food Chem 2000;71:301-8.
9. Van Ruth SM, Villenuve E. Influence of beta-lactoglobulin, pH and presence of other aroma compounds on the air/liquid partition coefficients of 20 aroma compounds varying in functional group and chain length. Food Chem 2002;79:157-64.
10. Landy P, et al. Retention of aroma compounds by proteins in aqueous solutions. Food Chem 1995;54:387-92.
11. Jasinski E, Kilara A. Flavour binding by whey proteins. Milchwissenschaft 1985;40:596-9.
12. Bucking M, Steinhart H. Characterization of the influence of different milk additives on the flavour release of coffee beverages by Headspace=GC and sensory analysis. J Agric Food Chem 2002;50:1529-34.
13. Kinsella JE. Functional properties of soy proteins. J Food Sci 1979;56:242-57.
14. Gremli HA. Interaction of flavour compounds with soy protein. Am Oil Chemists Soc 1974;51:95A-97A.
15. Damodaran S, Kinsella JE. Interactions of carbonyls with soy protein: thermodynamic effects. J Agric Food Chem 1981;29:1249-53.
16. Maheswari P, et al. Characterisation and application of porcine liver aldehyde oxidase in the off-flavour reduction of soy proteins. J Agric Food Chem 1997;45:2488-94.
17. Boatright WL, Lei Q. Headspace evaluation of methanethiol and dimethyl trisulfide in aqueous solutions of soy-protein. J Food Sci 2000;65:819-21.
18. Damodaran S, Kinsella JE. Interactions of carbonyls with soy protein: conformational effects. J Agric Food Chem 1981;29:1253-7.
19. Kim YD, Morr CV. Microencapsulation properties of gum Arabic and several food proteins: spray dried orange oil emulsion particles. J Agric Food Chem 1996;44:1314-20.
20. Kim H, Min DB. Interaction of flavour compounds with protein. In McGorrin Rj and Leland JV, Flavour-Food Interaction. ACS Symposium Series 1996;633:404-20.
21. Witty M. New technologies for taste modifying proteins. Trends Food Sci Technol 1998;9:275-80.
22. Gonzalez-Martinez C, et al. Influence of substituting milk powder for whey powder on yoghurt quality. Trends Food Sci Tech 2002;13:334-40.
23. Prakash V, Rao N. Physicochemical properties of oilseed proteins. CRC Crit Rev Biochem 1986;20:265-363.
24. Paredes-Lopez O. Safflower proteins for food use. In Hudson BJF, Developments in food proteins 7. New York. Elsevirer Applied Science 1991;1-33.
25. Lampart-Szczapa E. Legume and oilseed proteins. In Sikorski AE, Chemical and functional properties of food proteins. Lancaster, PA. Technoimic Publications 2001;407-36.
26. Marcone MF. Biochemical and biophysical properties of plant storage proteins: a current understanding with emphasis on 11S seed globulins. Food Res Int 1999;32:79-92.
27. Schwenke K, et al. Isolation of the 12S globulin from rapeseed (Brassica napus L) and characterization as a 'neutral' protein. On seed proteins. 13', Nahrung 1981;25:271-80.
28. El-Adawy TA. Effect of sesame seed protein supplementation on the nutritional, physical, chemical and sensory properties of wheat flour bread. Food Chem 1995;59:7-14.
29. Yue P, et al. Native and succinylated sunflower proteins use in bread baking. J Food Sci 1991;56:992-5.
30. Singh B, Singh U. Peanut as a source of protein in human foods. Plant Foods Human Nutr 1991;41:165-71.
31. Sotillo E, et al. Changes in starch and protein on extrusion of corn starch and sunflower protein blends. J Food Sci 1994;59:436-40.
32. El-Sayed MM. Use of plant protein isolates in processed cheese. Nahrung 1997;41:91-5.
33. Oomah BD, Mazza G. Flax proteins — a review. Food chem. 1993;48:109-14.
34. Villanueva A, et al. Peptide characteristics of sunflower protein hydrolysates. J Amer Oil Chem Soc 1999;76:1455-60.
35. Sessa DJ, Wing RE. Metal chelation of corn protein products/citric acid derivatives generated via reactive extrusion. Indus Crops Prod 1999;10:55-63.
36. Shahidi F. Beneficial health effect and drawbacks of antinutrients and phytochemicals in foods. In Shahidi F, Antinutrients and phytochemicals in foods. Washington DC, Amer Chem Soc (Symposium Series 662):1-9.

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