• John M. deMan
Part of the Food Science Text Series book series (FSTS)


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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  1. Aoki, T., et al. 1987. Caseins are cross-linked through their ester phosphate groups by colloidal calcium phosphate. Biochim. Biophys. Acta 911: 238–243.CrossRefGoogle Scholar
  2. Aschaffenburg, R. 1965. Variants of milk proteins and their pattern of inheritance. J. Dairy Sci. 48: 128–132.CrossRefGoogle Scholar
  3. 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.Google Scholar
  4. 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.Google Scholar
  5. 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.Google Scholar
  6. 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.CrossRefGoogle Scholar
  7. 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.Google Scholar
  8. Brooks, J.R., and C.V. Moor. 1985. Current aspects of soy protein fractionation and nomenclature. J. Am. Oil Chem. Soc. 62: 1347–1354.CrossRefGoogle Scholar
  9. 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.Google Scholar
  10. 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.Google Scholar
  11. Catsimpoolas, N. 1969. Isolation of glycinin subunits by isoelectric focussing in ureamercaptoethanol. FEBS Letters 4: 259–261.CrossRefGoogle Scholar
  12. Catsimpoolas, N., et al. 1967. Purification and structural studies of the 1 IS component of soybean proteins. Cereal Chem. 44: 631–637.Google Scholar
  13. Connell, J.J. 1962. Fish muscle proteins. In Recent advances in food science. Vol. 1, ed. J. Hawthorn and J.M. Leitch. London: Butterworth.Google Scholar
  14. Dalgleish, D.G. 1989. Protein-stabilized emulsions and their properties. In Water and food quality, ed. T.M. Hardman. London: Elsevier Applied Science Publishers.Google Scholar
  15. 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.Google Scholar
  16. 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.Google Scholar
  17. Farrell, H.M. 1973. Models for casein micelle formation. J. Dairy Sci. 56: 1195–1206.CrossRefGoogle Scholar
  18. 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.Google Scholar
  19. Finley, J.W., and W.F. Shipe. 1971. Isolation of a flavor producing fraction from light exposed milk. J. Dairy Sci. 54: 15–20.CrossRefGoogle Scholar
  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.Google Scholar
  21. Gross, J. 1961. Collagen Sci. Am. 204, no. 5: 120–130.Google Scholar
  22. 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.Google Scholar
  23. 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.CrossRefGoogle Scholar
  24. 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.Google Scholar
  25. 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.Google Scholar
  26. Hodge, J.E. 1953. Chemistry of browning reactions in model systems. Agr. Food Chem. 1: 928–943.CrossRefGoogle Scholar
  27. 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.Google Scholar
  28. 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.Google Scholar
  29. 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.Google Scholar
  30. 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.Google Scholar
  31. Kirchmeier, O. 1962. The physical-chemical causes of the heat stability of milk proteins (in German). Milchweissenschaft 17: 408–412.Google Scholar
  32. Krull, L.H., and J.S. Wall. 1969. Relationship of amino acid composition and wheat protein properties. Bakers' Dig. 43, no. 4: 30–39.Google Scholar
  33. Lasztity, R. 1996. The chemistry of cereal protein. 2nd ed. Boca Raton, FL: CRC Press.Google Scholar
  34. 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.Google Scholar
  35. 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.Google Scholar
  36. 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.Google Scholar
  37. Mauron, J. 1970. The chemical behavior of proteins during food preparation and its biological effect (in French). J. Vitamin Res. 40: 209–227.Google Scholar
  38. Mauron, J. 1983. Interaction between food constituents during processing. In Proceedings of the Sixth International Conference on Food Science Technology, 301–321. Dublin, Ireland.Google Scholar
  39. 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.CrossRefGoogle Scholar
  40. 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.Google Scholar
  41. Morr, C.V. 1984. Production and use of milk proteins in food. Food Technol. 38, no. 7: 39–48.Google Scholar
  42. 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.Google Scholar
  43. Nielsen, H.K., J. Loliger, and R.F. Hurrell. 1985. Reactions of proteins with oxidizing lipids. Brit. J. Nutr. 53: 61–73.CrossRefGoogle Scholar
  44. Patton, S. 1954. The mechanism of sunlight flavor formation in milk with special reference to methionine and riboflavin. J. Dairy Sci. 37: 446–452.CrossRefGoogle Scholar
  45. 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.CrossRefGoogle Scholar
  46. Paulsen, T.M., and F.E. Horan. 1965. Functional characteristics of edible soya flours. Cereal Sci. Today 10, no. 1: 14–17.Google Scholar
  47. 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.CrossRefGoogle Scholar
  48. Pomeranz, Y. 1968. Relationship between chemical composition and bread making potentialities of wheat flour. Adv. Food Research 16: 335–455.CrossRefGoogle Scholar
  49. Pomeranz, Y. 1991. Functional properties of food components. San Diego, CA: Academic Press.Google Scholar
  50. Poppe, J. 1992. Gelatin. In Thickening and gelling agents for food, ed. A. Imeson. London: Blackie Academic and Professional.Google Scholar
  51. Powrie, W.D. 1984. Chemical effects during storage of frozen foods. J. Chem. Educ. 61: 340–347.CrossRefGoogle Scholar
  52. Puski, G., and P. Melnychyn. 1968. Starch gel electrophoresis of soybean globulins. Cereal Chem. 45: 192–197.Google Scholar
  53. 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.Google Scholar
  54. 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.CrossRefGoogle Scholar
  55. Roos, Y.H., K. Jouppila, and B. Zielasko. 1996a. Non-enzymatic browning-induced water plasticization. J. Thermal Anal. 47: 1437–1450.CrossRefGoogle Scholar
  56. 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.Google Scholar
  57. 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.Google Scholar
  58. Schonberg, A., and R. Moubacher. 1952. The Strecker degradation of a-amino acids. Chem. Rev. 50: 261–277.CrossRefGoogle Scholar
  59. 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.Google Scholar
  60. 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.Google Scholar
  61. Swaisgood, H.E. 1982. Chemistry of milk protein. In Developments in dairy chemistry, ed. P. F. Fox. New York: Elsevier Applied Science Publishers.Google Scholar
  62. 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.Google Scholar
  63. 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.CrossRefGoogle Scholar
  64. Wall, J.S. 1971. Disulfide bonds: Determination, location and influence on molecular properties of proteins. Agr. Food Chem. 19: 619–625.CrossRefGoogle Scholar
  65. Wolf, W.J. 1969. Soybean protein nomenclature: A progress report. Cereal Sci. Today 14, no. 3: 75 –78, 129.Google Scholar
  66. Wolf, W.J. 1970. Scanning electron microscopy of soybean protein bodies. J. Am. Oil Chem. Soc. 47: 107108.Google Scholar
  67. 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.Google Scholar
  68. Wolf, W.J. 1972b. What is soy protein. Food Technol. 26, no. 5: 44–54.Google Scholar
  69. 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.CrossRefGoogle Scholar
  70. Ziegler, K. 1964. New cross links in alkali treated wool. J. Biol. Chem. 239: 2713–2714.Google Scholar

Copyright information

© Springer Science+Business Media New York 1999

Authors and Affiliations

  • John M. deMan
    • 1
  1. 1.Department of Food ScienceUniversity of GuelphGuelphCanada

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