Advertisement

Protein-Water Interactions

  • Marilynn I. Schnepf

Abstract

Water is one of the most important molecules necessary to sustain life. It is the only substance found in all three physical states. The interaction of water with other substances is critical to most chemical and biological reactions. Proteins also play an important role in many life processes. They provide structure to living cells and regulate many cellular functions. The interaction of these two important molecules plays an important role in determining the functional properties of many food ingredients. The focus of this chapter is to discuss the types of bonding which occur between water and protein molecules and to relate the interaction between water and protein molecules to the functional properties of proteins in foods.

Keywords

Protein Molecule Whey Protein Concentrate Water Binding Water Binding Capacity Protein Hydration 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Fennema, O., Water and Ice. In Food Chemistry, ed. O. Fennema. Marcel Dekker, Inc. NY, 1985, pp. 23–67.Google Scholar
  2. 2.
    Fennema, O., Water and protein hydration. In Food Proteins, ed. J. Whitaker & S. Tannenbaum. AVI, Westport CT, 1977, pp. 50–90.Google Scholar
  3. 3.
    Chou, D. & Morr, C., Protein-water interactions and functional properties. J. Am. Oil Chem. Soc., 56 (1979) 53A–62A.CrossRefGoogle Scholar
  4. 4.
    Bull, H. & Breese K., Protein hydration. II. Specific heat of egg albumin. Arch. Biochem. Biophys., 128 (1968) 497–502.CrossRefGoogle Scholar
  5. 5.
    Kuntz, I., The physical properties of water associated with biomolecules. In Water Relations of Foods, ed. R Duckworth, Academic Press, NY, (1975), pp. 93–109.Google Scholar
  6. 6.
    Franks, F., Water in aqueous solutions: recent advances. In Properties of Water in Foods, ed. D. Simatos & J. Multon. Martinus Nijhoff Publishers, Dordrecht, The Netherlands, 1985, pp. 1–23.CrossRefGoogle Scholar
  7. 7.
    Kauzmann, W., Some factors in the interpretation of protein denaturation. Adv. Protein Chem., 14 (1959) 1–63.CrossRefGoogle Scholar
  8. 8.
    Pomeranz, Y., Functional Properties of Food Components. Academic Press, Orlando, FL, 1985, p. 153.Google Scholar
  9. 9.
    Finney, J., Organization and function of water in protein crystals. In Water, A Comprehensive Treatise, ed. F. Franks. Plenum Press, NY, 1979, pp. 47–122.CrossRefGoogle Scholar
  10. 10.
    Warner, D., Theoretical studies of water in carbohydrates and proteins. In Water Activity: Influences on Food Quality, ed. L. Rockland & G. Steward. Academic Press, NY, 1981, pp. 435–465.Google Scholar
  11. 11.
    Bull, H. & Breese, K., Protein hydration. I. Bind sites. Arch. Biochem. Biophys., 128 (1968) 488–496.CrossRefGoogle Scholar
  12. 12.
    Labuza, T., The properties of water in relationship to water binding in foods, a review. J. Food Proc. Preser., 1 (2) (1977) 167–190.CrossRefGoogle Scholar
  13. 13.
    Franks, F., Water, ice and solutions of simple molecules in water relations of foods. In Water Relations in Food, ed. R. Duckworth. Academic Press, NY, 1975, pp. 3–22.Google Scholar
  14. 14.
    Kinsella, J., Milk proteins: physicochemical and functional properties. CRC Crit. Rev. Food Sci. Nutr., 21 (3) (1984) 197, 262.CrossRefGoogle Scholar
  15. 15.
    Chen, J., Piva, M. & Labuza, T., Evaluation of water binding capacity (WBC) of food fiber sources. J. Food Sci., 49 (1984) 59–63.CrossRefGoogle Scholar
  16. 16.
    Leeder, J. & Watt, I., The stoichiometry of water sorption by proteins. J. Colloid Interface Sci., 48 (1974) 339–344.CrossRefGoogle Scholar
  17. 17.
    Anderson, C. & Witter, L., Water binding capacity of 22 L-amino acids from water activity of 0.33 to 0.95. J. Food Sci., 47 (1982) 1952–1954.CrossRefGoogle Scholar
  18. 18.
    Kuntz, I., Hydration of macromolecules. III. Hydration of polypeptides. J. Am. Chem. Soc., 93 (1971) 514–516.CrossRefGoogle Scholar
  19. 19.
    Kuntz, I. & Brassfield, T., Hydration of macromolecules. II. Effects of urea on protein hydration. Arch. Biochem. Biophys., 142 (1971) 660–664.CrossRefGoogle Scholar
  20. 20.
    Tombs, M., Phase separation in protein-water systems and the formation of structure. In Properties of Water in Foods, ed. D. Simatos & J. Multon. Martinus Nijhoff Publishers, Dordrecht, The Netherlands, 1985, pp. 25–36.CrossRefGoogle Scholar
  21. 21.
    Shen, J., Solubility and Viscosity. In Protein functionality in foods, ed. J. Cherry. Am. Chem. Soc. Washington, D.C., 1981, pp. 89–109.CrossRefGoogle Scholar
  22. 22.
    Bingham, E., Influence of temperature and pH on the solubility of αs1,-β and κ-Casein. J. Dairy Sci., 54 (1971) 1077–1080.CrossRefGoogle Scholar
  23. 23.
    Shen, J., Soy protein solubility: The effect of experimental conditions on the solubility of soy protein isolates. Cereal Chem. 53 (6) (1976) 902–909.Google Scholar
  24. 24.
    German, B., Damodaran, S. & Kinsella, J., Thermal dissociation and association behaviour of soy proteins. J. Agric. Food Chem., 32, 807–811.Google Scholar
  25. 25.
    Bigelow, C., On the average hydrophobicity of proteins and the relation between it and protein structure. J. Theoret. Bio., 16 (1967) 187–211.CrossRefGoogle Scholar
  26. 26.
    Von Hippel, P. & Wong, K., The effect of ions on the kinetics of formation and stability of the collagen fold, 1 (1962) 664–674.Google Scholar
  27. 27.
    Bull, H. & Breese, K., Water and solute binding by proteins. II. Denaturants. Arch. Biochem. Biophys., 139 (1970) 93–96.CrossRefGoogle Scholar
  28. 28.
    Damodaran, S. & Kinsella, J., Effects of ions on protein conformation and functionality. In Protein Structure Deterioration, ed. J. Cherry. ACS Publication, Am. Chem. Soc., Washington, DC, 1982, pp. 327–356.CrossRefGoogle Scholar
  29. 29.
    Eagland, D., Protein hydration — its role in stabilizing the helix conformation of protein. In Water Relations of Foods, ed. R. Duckworth. Academic Press, NY, 1975, pp. 73–92.Google Scholar
  30. 30.
    Eagland, D., Nucleic acids, peptides and proteins. In Water, A comprehensive Treatise, ed. F. Franks. Plenum Press, NY, 1975, pp. 305–518.Google Scholar
  31. 31.
    Melander, W. & Horvath, C., Effect of neutral salts on the formation and dissociation of protein aggregates. J. Solid-Phase Biochem., 2 (2) (1977) 141–161.Google Scholar
  32. 32.
    Matsudomi, N., Mori, H., Kato, A. & Kobayashi, K., Emulsifying and foaming properties of heat-denatured soybean 115 globulins in relation to their surface hydrophobicity. Agric. Biol. Chem., 49 (4) (1985) 915–919.CrossRefGoogle Scholar
  33. 33.
    Schnepf, M. & Satterlee, L., Partial characterization of an iron soy protein complex. Nutr. Repts. Int., 31 (1985) 371–380.Google Scholar
  34. 34.
    Hardy, J. & Steinberg, M., Interaction between sodium chloride and paracasein as determined by water sorption. J. Food Sci., 49 (1984) 127–131.CrossRefGoogle Scholar
  35. 35.
    Konstance, R. & Strange, E., Solubility and viscous properties of casein and caseinates. J. Food Sci., 56 (1991) 556–559.CrossRefGoogle Scholar
  36. 36.
    Hamm, R., Water-holding capacity of meat. In Meat, ed. D. Cole & R. Lawrie. AVI Publishing Co., Inc. Westport, CT, 1975.Google Scholar
  37. 37.
    Berlin, E., Hydration of milk proteins. In Water Activity: Influences on Food Quality, ed. L. Rockland & G. Steward. Academic Press, NY, 1981, pp. 467–488.Google Scholar
  38. 38.
    Geankoplis, C., Transport Processes and Unit Operations. Allyn and Bacon, Inc., Boston, 1978, p. 46.Google Scholar
  39. 39.
    Richardson, S., Baiann, I. & Steinberg, M., Relation between oxygen-17 NMR and rheological characteristics of wheat flour suspension. J. Food Sci., 59 (1985) 1148–1151.CrossRefGoogle Scholar
  40. 40.
    Schmidt, R. & Morris, H., Gelation properties of milk proteins, soy proteins, and blended protein systems. Food Technol., 38 (5) (1984) 85–96.Google Scholar
  41. 41.
    Ziegler, G. & Acton, J., Mechanisms of gel formation by proteins of muscle tissue. Food Technol., 38 (5) (1984) 77–82.Google Scholar
  42. 42.
    O’Brien, S., Baker, R., Hood, L. & Liboff, M., Water-holding capacity and textural acceptability of precooked frozen white egg omelets. J. Food Sci., 47 (1982) 412–417.CrossRefGoogle Scholar
  43. 43.
    Burgarella, J., Lanier, T., Hamann, D. & Wu, M., Gel strength development during heating of surimi in combination with egg white or whey protein concentrate. J. Food Sci., 50 (1985) 1595–1597.CrossRefGoogle Scholar
  44. 44.
    Mulvihill, D. & Kinsella, J., Gelation characteristics of whey proteins and βlactoglobulin. Food Technol., 41 (9) (1987) 102–111.Google Scholar
  45. 45.
    Gossett, P., Rizvi, S. & Baker, R., Quantitative analysis of gelation in egg protein systems. Food Technol., 38 (5) (1984) 67–74, 96.Google Scholar
  46. 46.
    Hamm, K., The water imbibing power of foods. Rec. Adv. Food Sci., 31 (1963) 218.Google Scholar
  47. 47.
    Beveridge, T., Jones, L. & Tung, M., Progel and gel formation and reversibility of gelation of whey, soybean and albumen protein gels. J. Agric. Food Chem., 32 (1984) 307–313.CrossRefGoogle Scholar
  48. 48.
    Hegg, P., Conditions for the formation of heat-induced gels of some globular food proteins. J. Food Sci., 42 (1982) 1241–1244.CrossRefGoogle Scholar
  49. 49.
    Babajimopoulos, M., Damodaran, S., Rizvi, S. & Kinsella, J., Effects of various anions on the rheological and gelling behaviour of soy proteins: thermodynamic observations. J. Agric. Food Chem., 31 (1983) 1270.CrossRefGoogle Scholar
  50. 50.
    Utsumi, S. & Kinsella, J., Forces involved in soy protein gelation: Effects of various reagents on the fermenting hardness and solubility of heat-induced gels made from 7S, 11S, and soy isolate. J. Food Sci., 50 (1985) 1278–1282.CrossRefGoogle Scholar
  51. 51.
    Van Kleef, F., Thermally induced protein gelation: gelation and rheological characterization of highly concentrated ovalbumin and soybean protein gel. Biopolymers, 25 (1986) 31–59.CrossRefGoogle Scholar
  52. 52.
    O’Riordan, D., Morrissey, P., Kinsella, J. & Mulvihill, D., The effects of salts on the rheological properties of plasma protein gels. Food Chem., 34 (1989) 249–259.CrossRefGoogle Scholar
  53. 53.
    Schmidt, R., Gelation and coagulation. In Protein Functionality in Foods, ed. J. Cherry. Am. Chem. Soc. Washington, D.C., 1981, pp. 132–147.Google Scholar
  54. 54.
    Shimada, K. & Matsushita, S., Relationship between thermocoagulation of proteins and amino acid compositions. J. Agri. Food Chem., 28 (1980) 413–417.CrossRefGoogle Scholar
  55. 55.
    Goldsmith, S. & Toledo, R., Studies on egg albumin gelation using nuclear magnetic resonance. J. Food Sci., 50 (1985) 59–62.CrossRefGoogle Scholar
  56. 56.
    Labuza, T. & Busk, G., An analysis of the water binding in gels. J. Food Sci., 44 (1979) 1379–1394.CrossRefGoogle Scholar
  57. 57.
    Hermannsson, A. & Lucisano, M., Gel characteristics-waterbinding properties of blood plasma gels and methodological aspects on the water-binding of gel systems. J. Food Sci., 47 (1982) 1955–1959.CrossRefGoogle Scholar
  58. 58.
    Hermannsson, A. M., Gel characteristics-structure as related to texture and waterbinding of blood plasma gels. J. Food Sci., 47 (1982) 1965–1972.CrossRefGoogle Scholar
  59. 59.
    Gossett, P. & Baker, R., Effect of pH and of succinylation on the water retention properties of coagulated frozen and thawed egg albumin. J. Food Sci., 48 (1983) 1391–1394.CrossRefGoogle Scholar
  60. 60.
    Busk, G., Polymer-water interactions in gelation. Food Technol., 38 (5) (1984) 59–64.Google Scholar
  61. 61.
    Cheftel, J., Cug, J. & Lorient, D., Amino acids, peptides and proteins. In Food Chemistry, ed. O. Fennema. Marcel Dekker, Inc., NY, 1985, pp. 245–369,Google Scholar
  62. 61a.
    Cheftel, J., Cug, J. & Lorient, D., Amino acids, peptides and proteins. In Food Chemistry, ed. O. Fennema. Marcel Dekker, Inc., NY, 1985, pp. 303.Google Scholar
  63. 62.
    Graham, D. & Phillips, M., Proteins at liquid interfaces. V. Shear properties. J. Colloid Interface Sci., 76 (1980) 240–250.CrossRefGoogle Scholar
  64. 63.
    Graham, D. & Phillips, M., Proteins at liquid interfaces. I. Kinetics of adsorption and surface denaturation. J. Colloid Interface Sci., 70 (1979) 403–414.CrossRefGoogle Scholar
  65. 64.
    Halling, P., Protein stabilized foams and emulsions. CRC Crit. Rev. Food Sci. Nutr., 15 (1981) 155–203.CrossRefGoogle Scholar
  66. 65.
    Graham, D. & Phillips, M., Proteins at liquid interfaces. III. Molecular structure of adsorbed films. J. Colloid Interface Sci., 70 (1979) 427–439.CrossRefGoogle Scholar
  67. 66.
    Nakai, S., Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity. J. Agri. Food Chem., 31 (1983) 676–683.CrossRefGoogle Scholar
  68. 67.
    Townsend, A. & Nakai, S., Relationship between hydrophobicity and foaming characteristics of food proteins. J. Food Sci., 48 (1983) 588–594.CrossRefGoogle Scholar
  69. 68.
    Kato, A., Takahashi, A., Matsudomi, N. & Kobayashi, K., Determination of foaming properties of proteins by conductivity measurements. J. Food Sci., 48 (1983) 62–65.CrossRefGoogle Scholar
  70. 69.
    Hamm, R., The effect of the quality of meat and meat products: problems and research needs. In Properties of Water in Foods, ed. D. Simatos & J. Multon. Martinus Nijhoff Publishers, Dordrecht, The Netherlands, 1985, pp. 591–602.CrossRefGoogle Scholar
  71. 70.
    Blanchard, J. & Derbyshire, W., Physico-chemical studies of water in meat. In Water Relations of Foods, ed. R. Duckworth. Academic Press, NY, 1975, pp. 559–571.Google Scholar
  72. 71.
    Shults, G. & Wierbicki, E., Effects of sodiuim chloride and condensed phosphates on the water-holding capacity, pH and swelling of chicken muscle. J. Food Sci., 38 (1973) 991–994.CrossRefGoogle Scholar
  73. 72.
    Offer, G. & Trinick, J., On the mechanism of water holding in meat: The swelling and shrinking of myofibrils. Meat Sci., 8 (1983) 245–281.CrossRefGoogle Scholar
  74. 73.
    Shults, G., Russell, D. & Wierbicki, E., Effect of condensed phosphates on pH, swelling and water-holding capacity of beef. J. Food Sci., 32 (1972) 860–864.CrossRefGoogle Scholar
  75. 74.
    Trout, G. & Schmidt, G. The effect on cooking temperature on the functional properties of beef proteins: the role of ionic strength, pH, and pyrophosphate. Meat Sci., 20 (1987) 129–147.CrossRefGoogle Scholar
  76. 75.
    Labuza, T. & Saltmarch, M., The nonenzymatic browning reactions as affected by water in foods. In Water Activity: Influences on Food Quality, ed. L. Rockland & G. Steward. Academic Press, NY, 1981, pp. 605–650.Google Scholar
  77. 76.
    Eichner, K. & Ciner-Doruk, M., Formation and decomposition of browning intermediates and visible sugar-amine browning reactions. In Water Activity: Influences of Food, ed. L. Rockland & G. Steward. Academic Press, NY, 1975, 567–603.Google Scholar
  78. 77.
    Labuza, T. Water binding of humectants. In Properties of Water in Foods, ed. D. Simatos & J. Multon. Martinus Nijhoff Publishers,Dordrecht, The Netherlands, 1985, pp. 421–445.CrossRefGoogle Scholar
  79. 78.
    Eichner, K., Laible, R. & Wolf, W., The influence of water content and temperature on the formation of Maillard reaction intermediates during drying of plant products. In Properties of Water in Foods, ed. D. Simatos & J. Multon. Martinus Nijhoff Publishers, Dordrecht, The Netherlands, 1985, pp. 191–210.CrossRefGoogle Scholar
  80. 79.
    Wang, C. & Damodaran, S., Thermal destruction of cysteine and cystine residues of soy protein under conditions of gelation. J. Food Sci., 55 (1990) 1077–1080.CrossRefGoogle Scholar
  81. 80.
    Friedman, M., Levin, C. & Noma, A., Factors governing lysinoalanine formation in soy proteins. J. Food Sci., 49 (1984) 1282–1288.CrossRefGoogle Scholar
  82. 81.
    Rustad, T. & Nesse, N., Heat treatment and drying of capelin mince. Effect of water binding and soluble protein. J. Food Sci., 48 (1983) 1320–1322,CrossRefGoogle Scholar
  83. 81a.
    Rustad, T. & Nesse, N., Heat treatment and drying of capelin mince. Effect of water binding and soluble protein. J. Food Sci., 48 (1983), 1347.CrossRefGoogle Scholar
  84. 82.
    Kinsella, J., Functional properties of soy proteins. J. Am. Oil Chem. Soc., 56 (1979) 242–258.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media Dordrecht 1992

Authors and Affiliations

  • Marilynn I. Schnepf
    • 1
  1. 1.Department of Nutritional Science and Hospitality ManagementUniversity of NebraskaLincolnUSA

Personalised recommendations