Egg Proteins

Applied Food Protein Chemistry

Volumn 9781119944492, Issue , 2014, Pages 459-490

  Mine, Yoshinori ^a  

^a UNIVERSITY OF GUELPH   (Canada)

Author keywords

Avian eggs; Egg proteins; Emulsification; Foaming; Functionality; Gelation

Indexed keywords

EMULSIFICATION; GELATION;

AVIAN EGG; EGG PROTEIN; ESSENTIAL AMINO ACIDS; FOAMING; FOOD PROTEINS; FOOD SYSTEM; FUNCTIONAL PROPERTIES; FUNCTIONALITY; PROTEIN FUNCTIONALITIES; PROTEIN SOURCES;

PROTEINS;

EID: 84927797449     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9781118860588.ch17     Document Type: Chapter

References (160)

1. Alleoni, A.C.C. (2006). Albumen protein and functional properties of gelation and foaming. Sci Agric (Piracicaba, Braz) 63:291-298.
2. Alleoni, A.C.C. and Antunes, A.J. (2004). Albumen foam stability and s-ovalbumin contents in eggs coated with whey protein concentrate. Braz. J. Poult. Sci. 6:77-82.
3. Aluko, R.E. and Mine, Y. (1998). Characterization of oil-in-water emulsions stabilized by hen's egg yolk granule. Food Hydrocoll. 12:203-210.
4. Anfinsen, C.B. (1973). Principles that govern the folding of protein chains. Science 181:223-230.
5. Anton, M. (2007a). Composition and structure of hen egg yolk. In: Huopalahti, R., Lopez-Fandino, R., Anton, M., and Schade, R. (eds) Biactive Egg Compounds. Heidelberg, Germany: Springer. pp. 1-6.
6. Anton, M. (2007b). High-density lipoproteins (HDL) or lipovitellin fraction. In: Huopalahti, R., Lopez-Fandino, R., Anton, M., and Schade, R. (eds) Bioactive Egg Compounds. Heidelberg, Germany: Springer. pp. 13-16.
7. Anton, M. (2013). Egg yolk: structures, functionalities and processes. J. Sci. Food and Agric. doi:10.1002/jsfa.6247
8. Anton, M., Beaumal, V., and Gandemer, G. (2000). Adsorption at the oil-water interface and emulsifying properties of native granules from egg yolk: effect of aggregated state. Food Hydrocoll. 14:327-335.
9. Anton, M., Castellani, O., and Guerin-Dubiard, C. (2007). Phosvitin. In: Huopalahti, R., Lopez-Fandino, R., Anton, M., and Schade, R. (eds). Bioactive Egg Compounds. Heidelberg, Germany: Springer. pp. 16-24.
10. Anton, M. and Gandemer, G. (1997). Composition, solubility and emulsifying properties of granules and plasma of egg yolk. J. Food Sci. 62:484-487.
11. Anton, M. and Gandemer, G. (1999). Effect of pH on interface composition and on quality of oil-in-water emulsions made with hen egg yolk. Colloids Surf. B Biointerfaces 12:351-358.
12. Anton, M., Le Denmat, M., Beaumal, V., and Pilet, P. (2001). Filler effects of oil droplets on the rheology of heat-set emulsion gels prepared with egg yolk and egg yolk fractions. Food Hydrocoll. 21:137-147.
13. Anton, M., Martinet, V., Dalgalarrondo, M., Beaumal, V., David-Briand, E., and Rabesona H. (2003). Chemical and structural characterisation of low - density lipoproteins purified from hen egg yolk. Food Chem. 83:175-183.
14. Arntfield, S.D. and Bernatsky, A. (1993). Characteristic of heat-induced networks for mixtures of ovalbumin and lysozyme. J. Agric. Food Chem. 41:2291-2295.
15. Behn, I., Hommel, U., Erhard, M., Hlinak, A., Schade, R., Schwarzkopf, C., and Staak, C. (2001). Use of polyclonal avian antibodies. In: Schade, R., Behn, I., Erhard, M., Hlinak, A., and Staak, C. (eds) Chicken Egg Yolk Antibodies, Production and Application. New York: Springer. pp. 108-210.
16. Belitz, H.D., Grosch, W., and Schieberle, P. (2004a) Edible fats an oils. In: Food Chemistry. Heidelberg, Germany: Springer. pp. 643-672.
17. Belitz, H.D., Grosch, W., and Schieberle, P. (2004b) Eggs. Food Chemistry. Heidelberg, Germany: Springer. pp. 551-565.
18. Bolton, W. (1961). Chemical composition of eggs. In: Long, C. (ed) Biochemists' Handbook. London: E. & F.N. Spon Ltd. pp. 762-768.
19. Boye, J.I., Ma, C-Y., and Harwalkar, V.R. (1997). Thermal denaturation and coagulation of proteins. In: Damodaran, S. and Paraf, A. (eds) Food Proteins and Their Applications. New York: Marcel Dekker. pp. 25-56.
20. Burley, R.W. and Vadehra, D.V. (1989). The Avian Egg: Chemistry and Biology. New York: John Wiley and Sons, Inc. p. 472.
21. Burns, M.J. and Ackerman, C.J. (1955). Effect of dietary choline, methionine, and vit. B12 on weight and composition of eggs. Proc. Soc. Exp. Biol. Med. 89:420-421.
22. Campbell, L., Raikos, V., and Euston, S.R. (2003). Modification of functional properties of eggwhite proteins. Nahrung. 47:369-376.
23. Clark, A.H., Judge, F.J., Richards, J.B., Stubbs, J.M., and Suggett, A. (1981). Electron microscopy of network structures in thermally-induced globular protein gels. Int. J. Pept. Protein Res. 17: 380-392.
24. Cotterill, O.J., Chang, C.C., McBee, L.E., and Heymann, H. (1992). Metallic cations affect functional performance of spray-dried heat-treated egg white. J. Food Sci. 57:1321-1322.
25. Croguennec, T., Nau, F., Pezennec, S., and Brule, G. (2000). Simple rapid procedure for preparation of large quantities of ovalbumin. J. Agric. Food Chem. 48:4883-4889.
26. Croguennec, T., Renault, A., Beaufils, S., Dubois, J-J., and Pezennec, S. (2007). Interfacial properties of heat-treated ovalbumin. J. Colloid Interface Sci. 315:627-636.
27. Culbertson, J.D. (2012). Proteins: functional properties. In: Hui, Y.H. (ed) Food Chemistry: Principles and Application (3rd edn). West Sacramento: Science Technology Systems. pp. 9.1-9.14.
28. Damodaran, S. (1997a). Food proteins: an overview. In: Damodaran, S. and Paraf, A. (eds) Food Proteins and Their Applications. New York: Marcel Dekker. pp. 1-24.
29. Damodaran, S. (1997b). Protein-stabilized foams and emulsions. In: Damodaran, S. and Paraf, A. (eds) Food Proteins and Their Applications. New York: Marcel Dekker. pp. 57-110.
30. Damodaran, S. and Xu, S. (1996). The role of electrostatic forces in anomalous adsorption behavior of phosvitin at the air/water interface. J. Colloid Interface Sci. 178:426-435.
31. Dauphas, S., Beaumal, V., Gunning, P., Mackie, A., Wilde, P.V.V., and Riaublanc, A.M.A. (2007). Structure modification in hen egg yolk low density lipoproteins layers between 30 and 45 mN/m observed by AFM. Colloid Surf. B Biointerfaces 54:241-248.
32. Davis, J.P. and Foegeding, E.A. (2007). Comparisons of the foaming and interfacial properties of whey protein isolate and egg white proteins. Colloids Surf. B Biointerfaces 54:200-210.
33. DeMan, J.M. (1999). Principles of Food Chemistry (3rd edn). Gaithersburg, MD: Aspen Publishers.
34. Desert, C., Guérin-Dubiard, C., Nau, F., Jan, G., Val, F., and Mallard, J. (2001). Comparison of different electrophoretic separations of hen egg white proteins. J. Agric. Food Chem. 49:4553-4561.
35. Deutsch, H.F. and Morton, J.I. (1956). Immunochemical properties of heated ovomucoid. Arch. Biochem. Biophys. 64:19-25.
36. Deutsch, H.F. and Morton J.I. (1961). Physical-chemical studies of some modified ovomucoids. Arch. Biochem. Biophys. 93:654-660.
37. Doi, E. (1993). Gels and gelling of globular proteins, A review. Trends Food Sci. Technol. 4:1-3.
38. Doi, E. and Kitabatake, N. (1989). Structure of glycinin and ovalbumin gels. Food Hydrocoll. 3: 327-337.
39. Doi E. and Kitabatake, N. (1997). Structure and functionality of egg proteins. In: Damodaran, S. and Paraf, A. (eds) Food Proteins and Their Applications. New York: Marcel Dekker. pp. 325-340.
40. Doi, E., Kitabatake, N., Hatta, H., and Koseki, T. (1989). Relationship of SH groups to functionality of ovalbumin. In: Kinsella, J.E. and Soucie, W.G. (eds) Food Proteins. Champaign. IL: The American Oil Chemists's Society. pp. 252-266.
41. Du, L., Prokop, A., and Tanner, R.D. (2002). Effect of denaturation by preheating on the foam fractionation behavior of ovalbumin. J. Colloid Interface Sci. 248:487-492.
42. Forsythe, R.H. and Bergquist, D.H. (1951). The effect of physical treatments on some properties of egg white. Poultry Sci. 30:302-311.
43. Fothergill, L.A. and Fothergill, J.E. (1970). Thiol and disulphide contents of hen ovalbumin: C-terminal sequence and location of disulphide bond. Biochem. J. 116:555-561.
44. Gauthier, F., Saïd, B., and Renault, A. (2001). Modification of bovine β-lactoglobulin by glycation in a powdered state or in aqueous solution: adsorption at the air-water interface. Colloids Surf. B Biointerfaces 21:37-45.
45. Guérin-Dubiard, C., Pasco, M., Hietanen, A., Quiros del Bosque, A., Nau, F., and Croguennec, T. (2005). Hen egg white fractionation by ion-exchange chromatography. J. Chromatogr. 1090: 58-67.
46. Halling, P.J. (1981). Protein-stabilized foams and emulsions. Crit. Rev. Food Sci. Nutr. 15:155-203.
47. Hammershøj, M. and Qvist, K.B. (2001). Importance of hen age and egg storage time for egg albumen foaming. Lebensm-Wiss Technol. 34:118-120.
48. Hammershøj, M., Nebel, C., and Carstens, J.H. (2008). Enzymatic hydrolysis of ovomucin and effect on foaming properties. Food Res. Int. 41:522-531.
49. Handa, A., Hayashi, K., Shidara, H., and Kuroda, N. (2001). Correlation of the protein structure and gelling properties in dried egg white products. J. Agric. Food Chem. 49:3957-3964.
50. Hatta, H., Hagi, T., and Hirano, K. (1997). Chemical and physicochemical properties of hen eggs and their application in foods. In: Yamamoto, T., Juneja, L.R., Hatta, H., and Kim, M. (eds) Hen Eggs: Their Basic and Applied Science. Boca Raton: CRC Press. pp. 117-134.
51. Hatta, H., Kitabatake, N., and Doi, E. (1986). Turbidity and hardness of a heat-induced gel of hen egg ovalbumin. Agric. Biol. Chem. 50:2083-2089.
52. Hayakawa, S. and Nakai, S. (1985). Contribution of hydrophobicity, net charge and sulfhydryl groups to thermal properties of ovalbumin. Can. Inst. Food Sci. Technol. J. 18:290-295.
53. Hayakawa, S. and Nakamura, R. (1986). Optimization approaches to thermally induced egg white lysozyme gel. Agric. Biol. Chem. 50:2039-2046.
54. Hayakawa, S. and Sato, Y. (1976). Studies on the dissociation of the soluble ovomucin by sonication. Agric. Biol. Chem. 40:2397-2404.
55. Hermansson, A-M. (1988). Gel structure of food biopolymers. In: Blanshard, J.M.V. and Mitchell, J.R. (eds) Food Structure-Its Creation and Evaluation. London: Butterworth-Heinemann. pp. 25-40.
56. Hiidenhovi, J. (2007). Ovomucin. In: Huopalahti, R., Lopez-Fandino, R., Anton, M., and Schade, R. (eds) Bioactive Egg Compounds. Heidelberg: Springer. pp. 61-68.
57. Hirose, M. (1993). Molten globule state of food proteins. Trends Food Sci. Technol. 4:48-51.
58. Hirose, M., Oe, H., and Doi, E. (1986). Thiol-dependent gelation of egg-white. Agric. Biol. Chem. 50:59-64.
59. Huang, Q., Qui, N., Ma, M.H., Jin, Y.G., Yang, H., Geng, F., and Sun, S.H. (2012). Estimation of egg freshness using S-ovalbumin as an indicator. Poultry Sci. 91:739-743.
60. Huntington, J.A. and Stein, P.E. (2001). Structure and properties of ovalbumin. J. Chrom. B. 756:189-198.
61. Huopalahti, R., Lopez-Fernandino, R., Anton, M., and Rudiger, S. (2007). Bioactive Egg Compounds. Heidelberg, Berlin: Springer-Verlag. p. 298.
62. IEC, International Egg Commission, (2012). World egg production. https://www.internationalegg.com/corporate/eggindustry/details.asp?id=18 (accessed May 1, 2014)
63. Itoh, T., Miyazaki, J., Sugawara, H., and Adachi, S. (1987). Studies on the characterization of ovomucin and chalaza of the hen's egg. J. Food Sci. 52:1518-1521.
64. Johnson, T.M. and Zabik, M.E. (1981a) Egg albumin protein interactions in an angel food cake system. J. Food Sci. 46:1231-1236.
65. Johnson, T.M. and Zabik, M.E. (1981b) Gelation properties of albumen proteins, singly and in combination. Poultry Sci. 60:2071-2083.
66. Johnson, T.M. and Zabik, M.E. (1981c) Ultrastructural examination of egg albumen protein foams. J. Food Sci. 46:1237-1240.
67. Jolivet, P., Boulard, C., Beaumal, V., Chardot, T., and Anton, M. (2006). Protein components of low-density lipoproteins purified from hen egg yolk. J. Agric. Food Chem. 54:4424-4429.
68. Juneja, L.R. and Kim, M. (1997). Egg yolk proteins. In: Yamamoto, T., Juneja, L.R., Hatta, H., and Kim, M. (eds) Hen Eggs: Their Basic and Applied Science. New York: CRC press. pp. 73-98.
69. Kato, A., Fujimoto, K., Matsudomi, N., and Kobayashi, K. (1986). Protein flexibility and functional properties of heat-denatured ovalbumin and lysozyme. Agric. Biol. Chem. 50:417-420.
70. Kato, A., Ibrahim, H.R., Nakamura, S., and Kobayashi, K. (1994). New methods for improving the functionality of egg white proteins. In: Sim, J.S., and Nakai, S. (eds) Egg Uses and Processing Technologies. New Developments. Wallingford: CAB International. pp. 250-267.
71. Kato, A., Ibrahim, H.R., Watanabe, H., Honma, K., and Kobayashi, K. (1989). New approach to improve the gelling and surface functional properties of dried egg white by heating in dry state. J. Agric. Food Chem. 37:433-437.
72. Kato, A., Ibrahim, H.R., Watanabe, H., Honma, K., and Kobayashi, K. (1990a) Enthalpy of denaturation and surface functional properties of heated egg white proteins in the dry state. J. Food Sci. 55:1280-1283.
73. Kato, A., Miyauchi, N., Matsudomi, N., and Kobayashi, K. (1987a). The role of sialic acid in the functional properties of ovomucin. Agric. Biol. Chem. 51:641-645.
74. Kato, A., Miyazaki, S., Kawamoto, A., and Kobayashi, K. (1987b). Effects of phosphate residues on the excellent emulsifying properties of phosphoglycoprotein phosvitin. Agric. Biol. Chem. 51:2989-2994.
75. Kato, A., Oda, S., Yamanaka, Y., Matsudomi, N., and Kobayashi, K. (1985). Functional and structural properties of ovomucin. Agric. Biol. Chem. 49:3501-3504.
76. Kato, A., Sasaki, Y., Furuta, R., and Kobayashi, K. (1990b) Functional protein-polysaccharide conjugate prepared by controlled dry-heating of ovalbumin-dextran mixtures. Agric. Biol. Chem. 54:107-112.
77. Kato, A., Schrode, J., Kohr, W.J., and Laskowski, M.J. (1987c) Chicken ovomucoid: determination of its amino acid sequence, determination of the trypsin reactive site, and preparation of all three of its domains. Biochemistry 26:193-201.
78. Kato, A., Tsutsui, N., Matsudomi, N., Kobayashi, K., and Nakai, S. (1981). Effects of partial denaturation on surface properties of ovalbumin and lysozyme. Agric. Biol. Chem. 45:2755-2760.
79. Kim, K. and Setser, C.S. (1982). Foaming properties of fresh and commercially dried eggs in the presence of stabilizers and surfactants. Poultry Sci. 61:2194-2199.
80. Kinsella, J.E. (1976). Functional properties of proteins in food: a survey. Crit. Rev. Food Sci. Nutr. 7:219-280.
81. Kiosseoglou, V. (2003). Egg yolk protein gels and emulsions. Curr. Opin. Colloids Interface Sci. 8:365-370.
82. Kitabatake, N., Hatta, H., and Doi, E. (1987). Heat-induced and transparent gel prepared from hen egg ovalbumin in the presence of salt by a two-step heating method. Agric. Biol. Chem. 51:771-778.
83. Kitabatake, N., Indo, K., and Doi, E. (1989). Changes in interfacial properties of hen egg ovalbumin caused by freeze-drying and spray-drying. J. Agric. Food Chem. 37:905-910.
84. Knorr, D., Zenker, M., Heinz, V., and Lee, D-U. (2004). Application and potential of ultrasonics in food processing. Trends Food Sci. Technol. 15:261-266.
85. Koseki, T., Fukuda, T., Kitabatake, N., and Doi, E. (1989a). Characterization of linear polymers induced by thermal denaturation of ovalbumin. Food Hydrocoll. 3:135-148.
86. Koseki, T., Kitabatake, N., and Doi, E. (1989b). Irreversible thermal denaturation and formation of linear aggregates of ovalbumin. Food Hydrocoll. 3:123-134.
87. Kovacs-Nolan, J. and Mine, Y. (2004). Passive immunization through avian egg antibodies. Food Biotech. 18:39-62.
88. Kovacs-Nolan, J. and Mine, Y. (2012). Egg yolk antibodies for passive immunity. Annu. Rev. Food Sci. Technol. 3:163-182.
89. Kovacs-Nolan, J., Phillips, M., and Mine, Y. (2005). Advances in the value of eggs and egg components for human health. J. Agric. Food Chem. 53:8421-8431.
90. Kristinssen, H.G. (2006). University of Florida, Research Foundation, Inc. Feb 28. Methods of improving the properties of egg proteins. US patent 7,005,158.
91. Le Denmat, M., Anton, M., and Gandemer, G. (1999). Protein denaturation and emulsifying properties of plasma and granules of egg yolk as related to heat treatment. J. Food Sci. 64:194-197.
92. Lee, W.C. and Chen, T.C. (2002). Functional characteristics of egg white solids obtained from papain treated albumen. J. Food Eng. 51:263-266.
93. Lechevalier, V., Croguennec, T., Nau, F., and Guerin-Dubiard, C. (2007). Ovalbumin and generelated proteins. In: Huopalahti, R., Lopez-Fandino, R., Anton, M., and Schade, R. (eds) Bioactive Egg Compounds. Heidelberg, Germany: Springer. pp. 51-60.
94. Li-Chan, E.C.Y. and Kim, H.O. (2008). Structure and chemical composition of eggs. In: Mine, Y. (ed) Egg Bioscience and Biotechnology. Hoboken, NY: John Wiley & Sons, Inc. pp. 1-95.
95. Li-Chan, E. and Nakai, S. (1989). Biochemical basis for the properties of egg white. Crit. Rev. Poult. Biol. 2:21-58.
96. Li-Chan, E. and Nakai, S. (1991). Raman spectroscopy study of thermally and/or dithiothreitol induced gelation of lysozyme. J. Agric. Food Chem. 39:1238-1245.
97. Li-Chan, E., Powrie, W.D., and Nakai, S. (1995). The chemistry of egg and egg products. In: Stadelman, W.J. and Cotterill, O.J. (eds) Egg Science and Technology. New York: Food Products Press. pp. 105-176.
98. Liang, Y. and Kristinsson, H.G. (2005). The influence of pH-induced unfolding and refolding of egg albumin on its foaming properties. J. Food Sci. 70:222-230.
99. Lomakina, K. and Mikova, K. (2006). A study of the factors affecting the foaming properties of egg white - a review. Czech. J. Food Sci. 24:110-118.
100. Longsworth, L.G., Cannan, R.K., and MacInnes, D.A. (1940). An electrophoretic study of the proteins of egg white. J. Am. Chem. Soc. 62:2580-2590.
101. Ma, C-Y., Poste, L.M., and Holme, J. (1986). Effects of chemical modifications on the physicochemical and cake-baking properties of egg white. Can. I. Food Sci. Tech. J. 19:17-22.
102. Ma, C-Y., Sahasrabudhe, M.R., Poste, L.M., Harwalkar, V.R., Chambers, J.R., and O'Hara, K.P.J. (1994). Gamma irradiation and physicochemical properties of eggs and egg products. In: Sim, J.S. and Nakai, S. (eds) Egg Uses and Processing Technologies. New Developments. Wallingford: CAB International. pp. 283-299.
103. MacDonnel, L.R., Feeney, R.E., Hanson, H.L., Campbell, A., and Sugihara, T.F. (1955). The functional properties of the egg white proteins. Food Technol. 9:49-53.
104. Mackie, A.R., Gunning, A.P., Wilde, P.J., and Morris, V.J. (1999). Orogenic displacement of protein from the air/water interface by competitive adsorption. J. Colloid Interface Sci. 210:157-166.
105. Mangino, M.E. (1994). Protein interactions in emulsions: protein-lipid interactions. In: Hettiarachchy, N.S. and Ziegler, G.R. (eds) Protein Functionality in Food Systems. New York: Marcel Dekker. pp. 147-180.
106. Martin, W.G., Augustyniak, J., and Cook, W.H., (1964). Fractionation and characterization of the low-density lipoproteins of hen's egg yolk. Biochim. Biophys. Acta 84:714-720.
107. Martinet, V., Beaumal, V., Dalgalarrondo, M., and Anton, M. (2002). Emulsifying properties and adsorption behaviour of egg yolk lipoproteins (LDL and HDL) in oil-in-water emulsions. In: Anton, M. (ed) Food Emulsions and Dispersions. Trivandrum: Research Signpost. pp. 103-116.
108. Martinet, V., Saulnier, P., Beaumal, V., Courthaudon, J.L., and Anton, M. (2003). Surface properties of hen egg yolk low-density lipoproteins spread at the air-water interface. Colloids Surf. B Biointerfaces 3:185-194.
109. Mel'nikov, S.M. (2002). Effect of pH on the adsorption kinetics of egg yolk at the triacylglycerolwater interface and viscoelastic properties of interfacial egg yolk films: a dynamic drop tensiometry study. Colloid Surf. B 27:265-275.
110. Messier, P. (1991). Protein chemistry of albumen photographs. Topics in Photographic Preservation 4:124-135.
111. Mine, Y. (1995). Recent advances in the understanding of egg white protein functionality. Trends Food Sci. Technol. 6:225-232.
112. Mine, Y. (1996). Laser light scattering study on the heat-induced ovalbumin aggregates related to its gelling property. J. Agric. Food Chem. 44:2086-2090.
113. Mine, Y. (1997). Effect of dry heat and mild alkaline treatment on functional properties of egg white proteins. J. Agric. Food Chem. 45:2924-2928.
114. Mine, Y. (2002). Recent advances in egg protein functionality in the food system. World Poultry Sci. J. 58:31-39.
115. Mine, Y., Noutomi, T., and Haga, N. (1991). Emulsifying and structural properties of ovalbumin. J. Agric. Food Chem. 39:443-446.
116. Mine, Y. and Yang, M. (2007). Epitope characterization of ovalbumin in BALB/c mice using different entry routes. Biochim. Biophys. Acta 1774:200-212.
117. Mleko, S., Kristinsson, H.G., Liang, Y., and Gustaw, W. (2007). Rheological properties of foams generated from egg albumin after pH treatment. Lebensm-Wiss Technol. 40:908-914.
118. Murray, B.S. (2007). Stabilization of bubbles and foams. Curr. Opin. Colloid Interface Sci. 12: 232-241.
119. Murray, B.S. and Ettelaie, R. (2004). Foam stability: proteins and nanoparticles. Curr. Opin. Colloid Interface Sci. 9:314-320.
120. Nakamura, R. and Doi, E. (2000). Egg processing. In: Nakai, S. and Modler, H.W. (eds) Food Proteins. Processing Applications. New York: Wiley-VCH. pp. 171-207.
121. Nakamura, R. and Sato, Y. (1964a). Studies on the foaming property of the chicken egg white. Part IX. On the coagulated proteins under various whipping conditions (The mechanism of foaminess). Biol. Chem. 38:524-529.
122. Nakamura, R. and Sato, Y. (1964b). Studies on the foaming property of the chicken egg white. Part X. On the role of ovomucin (B) in the egg white foaminess (The mechanism of foaminess). Agric. Biol. Chem. 28:530-534.
123. Nisbet, A.D., Saundry, R.H., Moir, A.J., Fothergill, L.A., and Fothergill, J.E. (1981). The complete amino-acid sequence of hen ovalbumin. Eur. J. Biochem. 115:335-345.
124. Oakenfull, D., Pearce, J., and Burley, R.W. (1997). Protein gelation. In: Damodaran, S. and Paraf, A. (eds) Food Proteins and Their Applications. New York: Marcel Dekker. pp. 111-142.
125. Oe, H., Hirose, M., and Doi, E. (1986). Conformation changes and subsequent gelation of conalbumin by a thiol reagent. Agric. Biol. Chem. 50:2469-2475.
126. Ohgushi, M. and Wada, A. (1983). 'Molten-globule state': a compact form of globular proteins with mobile side chains. FEBS Lett. 164:21-24.
127. Ottesen, M. and Wallevik, K. (1968). Use of the pH-stat for measuring the denaturation of ovalbumin in acid solutions. Biochim. Biophys. Acta 160:262-264.
128. Paraskevopoulou, A., Kiosseoglou, V., Alevisopoulos, S., and Kasapis, S. (2000). Small deformation measurements of single and mixed gels of low cholesterol yolk and egg white. J. Texture Studies 31:225-244.
129. Parkinson, T.L. (1966). The chemical composition of eggs. J. Sci. Food Agric. 17:101-111.
130. Phillips, L.G., Haque, Z., and Kinsella, J.E. (1987). A method for the measurement of foam formation and stability. J. Food Sci. 52:1074-1077.
131. Phillips, L.G., Whitehead, D.M., and Kinsella, J.E. (1994). Structure-Function Properties of Food Proteins. San Diego: Academic Press. p. 271.
132. Pour-El, A. (1981). Protein functionality: classification, definition and methodology. In: Pour-El, A. (ed) Protein Functionality in Foods. ACS Symposium Series Vol. 147. Washington: American Chemical Society. p. 5.
133. Raikos, V., Campbell, L., and Euston, S.R. (2007). Rheology and texture of hen's egg protein heatset gels as affected by pH and the addition of sugar and/or salt. Food Hydrocoll. 21:237-244.
134. Réhault, S. (2007). Antiproteases. In: Huopalahti, R., Lopez-Fandino, R., Anton, M., and Schade, R. (eds) Bioactive Egg Compounds. Heidelberg, Germany: Springer. pp. 85-92.
135. Rupa, P. and Mine, Y. (2006). Ablation of ovomucoid-induced allergic response by desensitization with recombinant ovomucoid third domain in a murine model. Clin. Exp. Immunol. 145:493-501.
136. Rupa, P., Nakamura, S., and Mine, Y. (2007). Genetically glycosylated ovomucoid third domain can modulate Immunoglobulin E antibody production and cytokine response in BALB/c mice. Clin. Exp. Allergy 37:918-928.
137. Saari, A., Powrie, W.D., and Fennema, O. (1964). Isolation and characterization of low-density lipoproteins in native egg yolk plasma. J. Food Sci. 29:307-315.
138. Schade, R. and Chacana, P. A. (2007). Livetin fractions (IgY). In: Huopalahti, R., Lopez-Fandino, R., Anton, M. and Schade, R. (ed) Bioactive Egg Compounds. Heidelberg, Germany: Springer. pp. 25-32.
139. Silversides, F.G. and Budgell, K. (2004). The relationships among measures of egg albumen height, pH, and whipping volume. Poult. Sci. 83:1619-1623.
140. Sirvente, H., Beaumal, V., Gaillard, C., Bialek, L., Hamm, D., and Anton, M. (2007). Structuring and functionalization of dispersions containing egg yolk, plasma and granules induced by mechanical treatments. J. Agric. Food Chem. 5:9537-9544.
141. Smith, D.M. (1994). Protein interactions in gels: protein-protein interactions. In: Hettiarachchy, N.S., and Ziegler, G.R. (eds) Protein Functionality in Food Systems. New York: Marcel Dekker. pp. 209-224.
142. Speroni, F., Puppo, M.C., Chapleau, N., de Lamballerie, M., Castellani, O.,Añón, M.C., and Anton, M. (2005). High-pressure induced physicochemical and functional modifications of low-density lipoproteins from hen egg yolk. J. Agric. Food Chem. 53:5719-5725.
143. Stadelman, W.J. and Cotterill, O.J. (1973). Egg Science and Technology. Westport Avi Publishing. p. 314.
144. Stein, P.E., Leslie, A.G.W., Finch, J.T., and Carrell, R.W. (1991). Crystal structure of uncleaved ovalbumin at 1.95 Å resolution. J. Molec. Biol. 221:941-959.
145. Sugino, H., Nitoda, T., and Juneja, L.R. (1997). General chemical composition of hen eggs. In: Yamamoto, T., Juneja, L.R., Hatta, H., and Kim, M. (eds) Hen Eggs: Their Basic and Applied Science. New York: CRC Press. pp. 13-24.
146. Superti, F., Ammendolia, M.G., Berlutti, F., and Valenti, P. (2007). Ovotransferrin. In: Huopalahti, R., Lopez-Fandino, R., Anton, M., and Schade, R. (eds) Bioactive Egg Compounds. Heidelberg, Germany: Springer. pp. 43-50.
147. Tani, F., Murata, M., Higasa, T., Goto, M., Kitabatake, N., and Doi, E. (1993). Heat-induced transparent gel from hen egg lysozyme by a two-step heating method. Biosci. Biotech. Biochem. 57:209-214.
148. Tani, F., Murata, M., Higasa, T., Goto, M., Kitabatake, N., and Doi, E. (1995). Molten globule state of protein molecules in heat-induced transparent food gels. Biosci. Biotech. Biochem. 43: 2325-2331.
149. Vadehra, D.V. and Nath, K. (1973). Eggs as a source of protein. CRC Crit. Rev. Food Technol. 4:193-309.
150. Walsh, B.J., Barnett, D., Burley, R.W., Elliott, C., Hill, D.J., and Howden, M.E. (1988). New allergens from hen's egg white and egg yolk. In vitro study of ovomucin, apovitellenin I and VI, and phosvitin. Int. Arch. Allergy Appl. Immunol. 87:81-86.
151. Walsh, B.J., Hill, D.J., Macoun, P., Cairns, D., and Howden, M.E. (2005). Detection of four distinct groups of hen egg allergens binding IgE in the sera of children with egg allergy. Allergol. Immunopathol. (Madr). 33:183-191.
152. Walstra, P. (1996). Dispersed systems: basic considerations. In: Fennema, O.R. (ed) Food Chemistry. New York: Marcel Dekker. pp. 95-155.
153. Wang, G. and Wang, T. (2009). Effects of yolk contamination, shearing, and heating on foaming properties of fresh egg white. J. Food Sci. 74(2):C147-C156.
154. Watanabe, K., Tsuge, Y., Shimoyamada, M., Onizuka, T., Niwa, M., Ido, T., and Tsuge, Y. (2004). Amino acid sequence of alpha-ovomucin in hen egg white ovomucin deduced from cloned cDNA. DNA Seq. 15:251e261.
155. Watkins, B.A. (1995). The nutritive value of the egg. In: Stadelman, W.J. and Cotterill, O.J. (eds) Egg Science and Technology. New York: Food Products Press. pp. 177-194.
156. Williams, J. (1962). Serum proteins and the livetins in hen's-egg yolk. Biochem. J. 83:346e355.
157. Williams, J. (1982). The evolution of transferrin. Trends Biochem. Sci. 7:394-397.
158. Woodward, S.A. (1990). Egg protein gels. In: Harris, P. (ed) Food Gels. New York: Elsevier. pp. 175-200.
159. Yang, S-C. and Baldwin, R.E. (1995). Functional properties of eggs in foods. In: Stadelman, W.J. and Cotterill, O.J. (eds) Egg Science and Technology. New York: Haworth Press. pp. 405-464.
160. Zhu, H. and Damodaran, S. (1994). Heat-induced conformational changes in whey protein isolate and its relation to foaming properties. J. Agric. Food Chem. 42:846-855.