Abstract
Proteins are polymers of some 21 different amino acids joined together by peptide bonds. Because of the variety of side chains that occur when these amino acids are linked together, the different proteins may have different chemical properties and widely different secondary and tertiary structures. The various amino acids joined in a peptide chain are shown in Figure 3-1. The amino acids are grouped on the basis of the chemical nature of the side chains (Krull and Wall 1969). The side chains may be polar or non- polar. High levels of polar amino acid residues in a protein increase water solubility. The most polar side chains are those of the basic and acidic amino acids. These amino acids are present at high levels in the soluble albumins and globulins. In contrast, the wheat proteins, gliadin and glutenin, have low levels of polar side chains and are quite insoluble in water. The acidic amino acids may also be present in proteins in the form of their amides, glutamine and asparagine. This increases the nitrogen content of the protein. Hydroxyl groups in the side chains may become involved in ester linkages with phosphoric acid and phosphates. Sulfur amino acids may form disulfide cross-links between neighboring peptide chains or between different parts of the same chain. Proline and hydroxyproline impose significant structural limitations on the geometry of the peptide chain.
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References
Aoki, T., et al. 1987. Caseins are cross-linked through their ester phosphate groups by colloidal calcium phosphate. Biochim. Biophys. Acta 911: 238–243.
Aschaffenburg, R. 1965. Variants of milk proteins and their pattern of inheritance. J. Dairy Sci. 48: 128–132.
Bailey, A.J. 1982. Muscle proteins and muscle structure. In Food proteins, ed. P.F. Fox and J.J. Condon. New York: Applied Science Publishers.
Barbut, S. 1994. Protein gel ultrastructure and functionality. In Protein functionality in food systems, ed. N.S. Hettiarachachy and G.R. Ziegler. New York: Marcel Dekker Inc.
Bietz, J.A., and J.S. Wall. 1972. Wheat gluten subunits: Molecular weights determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Cereal Chem. 49: 416–430.
Bjarnason, J., and K.J. Carpenter. 1970. Mechanisms of heat damage in proteins. 2. Chemical changes in pure proteins. Brit. J. Nutr. 24: 313–329.
Bodwell, C.E., and P.E. McClain. 1971. Proteins. In The science of meat and meat products, ed. J.F. Price and B.S. Schweigert. San Francisco: W.H. Freeman and Co.
Brooks, J.R., and C.V. Moor. 1985. Current aspects of soy protein fractionation and nomenclature. J. Am. Oil Chem. Soc. 62: 1347–1354.
Burton, H.S., and D.J. McWeeney. 1964. Non-enzymatic browning: Routes to the production of melanoidins from aldoses and amino compounds. Chem. Ind. 11: 462–463.
Cassens, R.G. 1971. Microscopic structure of animal tissues. In The science of meat and meat products, ed. J.F. Price and B.S. Schweigert. San Francisco: W.H. Freeman and Co.
Catsimpoolas, N. 1969. Isolation of glycinin subunits by isoelectric focussing in ureamercaptoethanol. FEBS Letters 4: 259–261.
Catsimpoolas, N., et al. 1967. Purification and structural studies of the 1 IS component of soybean proteins. Cereal Chem. 44: 631–637.
Connell, J.J. 1962. Fish muscle proteins. In Recent advances in food science. Vol. 1, ed. J. Hawthorn and J.M. Leitch. London: Butterworth.
Dalgleish, D.G. 1989. Protein-stabilized emulsions and their properties. In Water and food quality, ed. T.M. Hardman. London: Elsevier Applied Science Publishers.
deMan, J.M., L. deMan, and S. Gupta. 1986. Texture and microstructure of soybean curd (tofu) as affected by different coagulants. Food Microstructure 5: 83–89.
Ellis, G.P. 1959. The Maillard reaction. In Advances in carbohydrate chemistry. Vol. 14, ed. M.L. Wolfrom and R.S. Tipson. New York: Academic Press.
Farrell, H.M. 1973. Models for casein micelle formation. J. Dairy Sci. 56: 1195–1206.
Farrell, H.M., and M.P. Thompson. 1974. Physical equilibria: Proteins. In Fundaments of dairy chemistry., ed. B.H. Webb et al. Westport, CT: AVI Publishing Co.
Finley, J.W., and W.F. Shipe. 1971. Isolation of a flavor producing fraction from light exposed milk. J. Dairy Sci. 54: 15–20.
Gordon, W.G., and E.B. Kalan. 1974. Proteins of milk. In Fundamentals of dairy chemistry, ed. B.H. Webb et al. Westport, CT: AVI Publishing Co.
Gross, J. 1961. Collagen Sci. Am. 204, no. 5: 120–130.
Hamaker, B.R. 1994. The influence of rice protein on rice quality. In Rice science and technology, ed. W.E. Marshall and J.I. Wadsworth. New York: Marcel Dekker.
Harland, H.A., S.T. Coulter, and R. Jenness. 1952. The effect of various steps in the manufacture on the extent of serum protein denaturation in nonfat dry milk solids. J. Dairy Sci. 35: 363–368.
Hatta, H., and T. Koseki. 1988. Relationship of SH groups to functionality of ovalbumin. In Food proteins, ed. J.E. Kinsella and W.G. Soucie. Champaign, IL: American Oil Chemistry Society.
Hermansson, A.M. 1973. Determination of functional properties of protein foods. In Proteins in human nutrition, ed. J.W.G. Porter and B.A. Rolls. London: Academic Press.
Hodge, J.E. 1953. Chemistry of browning reactions in model systems. Agr. Food Chem. 1: 928–943.
Hodge, J.E., F.D. Mills, and B.E. Fisher. 1972. Compounds of browned flavor from sugar-amine reactions. Cereal Sci. Today 17: 34–40.
Hurrell, R.F. 1984. Reactions of food proteins during processing and storage and their nutritional consequences. In Developments in food proteins, ed. B.J.F. Hudson. New York: Elsevier Applied Science Publishers.
Hurst, D.T. 1972. Recent developments in the study of nonenzymic browning and its inhibition by sulphur dioxide. BFMIRA Scientific and Technical Surveys No. 75. Leatherhead, England.
Kinsella, J.E. 1982. Structure and functional properties of food proteins. In Food proteins, ed. P.F. Fox and J.J. Condon. New York: Applied Science Publishers.
Kirchmeier, O. 1962. The physical-chemical causes of the heat stability of milk proteins (in German). Milchweissenschaft 17: 408–412.
Krull, L.H., and J.S. Wall. 1969. Relationship of amino acid composition and wheat protein properties. Bakers' Dig. 43, no. 4: 30–39.
Lasztity, R. 1996. The chemistry of cereal protein. 2nd ed. Boca Raton, FL: CRC Press.
Lookhart, G.L. 1991. Cereal proteins: Composition of their major fractions and methods of identification. In Handbook of cereal science and technology, ed. K.J. Lorenz and K. Kulp. New York: Marcel Dekker.
Mackie, I.M. 1983. New approaches in the use of fish proteins. In Developments in food proteins, ed. B.J.F. Hudson. New York: Applied Science Publishers.
Masters, P.M., and M. Friedman. 1980. Amino acid racemization in alkali-treated food proteins: Chemistry, toxicology and nutritional consequences. In Chemical deterioration of proteins, ed J.R. Whitaker and M. Fujimaki. Americal Chemical Society Symposium Series 123. Washington, DC: American Chemical Society.
Mauron, J. 1970. The chemical behavior of proteins during food preparation and its biological effect (in French). J. Vitamin Res. 40: 209–227.
Mauron, J. 1983. Interaction between food constituents during processing. In Proceedings of the Sixth International Conference on Food Science Technology, 301–321. Dublin, Ireland.
Mertz, E., O. Nelson, and L.S. Bates. 1964. Mutant gene that changes composition and increases lysine content of maize endosperm. Science 154: 279–280.
Mitchell, J.R. 1986. Foaming and emulsifying properties of proteins. In Developments in food proteins, ed. B.J.F. Hudson. New York: Elsevier Applied Science Publishers.
Morr, C.V. 1984. Production and use of milk proteins in food. Food Technol. 38, no. 7: 39–48.
Nakai, S., and W.D. Powrie. 1981. Modification of proteins for functional and nutritional improvements. In Cereals: A renewable resource, theory and practice, ed. Y. Pomeranz and L. Munck. St. Paul, MN: American Association of Cereal Chemistry.
Nielsen, H.K., J. Loliger, and R.F. Hurrell. 1985. Reactions of proteins with oxidizing lipids. Brit. J. Nutr. 53: 61–73.
Patton, S. 1954. The mechanism of sunlight flavor formation in milk with special reference to methionine and riboflavin. J. Dairy Sci. 37: 446–452.
Pauling, L., R.B. Corey, and H.R. Branson. 1951. The structure of proteins: Two hydrogen bonded helical configurations of the polypeptide chain. Proc. Natl. Acad. Sci. (US) 37: 205–211.
Paulsen, T.M., and F.E. Horan. 1965. Functional characteristics of edible soya flours. Cereal Sci. Today 10, no. 1: 14–17.
Peterson, R.F., L.W. Nauman, and T.L. McMeekin. 1958. The separation and amino acid composition of a pure phosphopeptone prepared from p-casein by the action of trypsin. J. Am. Chem. Soc. 80: 95–99.
Pomeranz, Y. 1968. Relationship between chemical composition and bread making potentialities of wheat flour. Adv. Food Research 16: 335–455.
Pomeranz, Y. 1991. Functional properties of food components. San Diego, CA: Academic Press.
Poppe, J. 1992. Gelatin. In Thickening and gelling agents for food, ed. A. Imeson. London: Blackie Academic and Professional.
Powrie, W.D. 1984. Chemical effects during storage of frozen foods. J. Chem. Educ. 61: 340–347.
Puski, G., and P. Melnychyn. 1968. Starch gel electrophoresis of soybean globulins. Cereal Chem. 45: 192–197.
Ranken, M.D. 1984. Composition of meat: Some structural and analytical implications. In Developments in food proteins, ed. B.J.F. Hudson. New York: Elsevier Applied Science Publishers.
Roos, Y.H., and M. Himberg. 1994. Non-enzymatic browning behavior, as related to glass transition, of a model at chilling temperatures. J. Agr. Food Chem. 42: 893–898.
Roos, Y.H., K. Jouppila, and B. Zielasko. 1996a. Non-enzymatic browning-induced water plasticization. J. Thermal Anal. 47: 1437–1450.
Roos, Y.H., M. Karel, and J.L. Kokini. 1996b. Glass transitions in low moisture and frozen foods: Effect on shelf life and quality. Food Technol. 50 (10): 95108.
Schofield, J.D., and M.R. Booth. 1983. Wheat proteins and their technological significance. In Developments in food proteins, ed. B.J.F. Hudson. New York: Elsevier Applied Science Publishers.
Schonberg, A., and R. Moubacher. 1952. The Strecker degradation of a-amino acids. Chem. Rev. 50: 261–277.
Simmonds, D.H., and R.A. Orth. 1973. Structure and composition of cereal proteins as related to their potential industrial utilization. In Industrial uses of cereals, ed. Y. Pomeranz. St. Paul, MN: American Association of Cereal Chemists.
Stanley, D.W., and R.Y. Yada. 1992. Thermal reactions in food protein systems. In Physical chemistry of foods, ed. H.G. Schwartzberg and R.W. Hartel. New York: Marcel Dekker, Inc.
Swaisgood, H.E. 1982. Chemistry of milk protein. In Developments in dairy chemistry, ed. P. F. Fox. New York: Elsevier Applied Science Publishers.
Swaisgood, H.E. 1995. Protein and amino acid composition of bovine milk. In Handbook of milk composition, ed. R.G. Jensen. New York: Academic Press, Inc.
Thomas, R, J.M. deMan, and L. deMan. 1989. Soymilk and tofu properties as influenced by soybean storage conditions. J. Am. Oil Chem. Soc. 66: 777–782.
Wall, J.S. 1971. Disulfide bonds: Determination, location and influence on molecular properties of proteins. Agr. Food Chem. 19: 619–625.
Wolf, W.J. 1969. Soybean protein nomenclature: A progress report. Cereal Sci. Today 14, no. 3: 75 –78, 129.
Wolf, W.J. 1970. Scanning electron microscopy of soybean protein bodies. J. Am. Oil Chem. Soc. 47: 107108.
Wolf, W.J. 1972a. Purification and properties of the proteins. In Soybeans: Chemistry and technology, ed. A.K. Smith and S.J. Circle. Westport, CT: AVI Publishing Co.
Wolf, W.J. 1972b. What is soy protein. Food Technol. 26, no. 5: 44–54.
Wong, D.W.S., W.M. Camirand, and A.E. Pavlath. 1996. Structures and functionalities of milk proteins. Crit. Rev. Food Sci. Nutr. 36: 807–844.
Ziegler, K. 1964. New cross links in alkali treated wool. J. Biol. Chem. 239: 2713–2714.
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deMan, J.M. (1999). Proteins. In: Principles of Food Chemistry. Food Science Text Series. Springer, Boston, MA. https://doi.org/10.1007/978-1-4614-6390-0_3
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