Milk Proteins

Applied Food Protein Chemistry

Volumn 9781119944492, Issue , 2014, Pages 427-458

  Farkye, Nana Y ^a   Shah, Nagendra ^b  

^a CALIFORNIA POLYTECHNIC STATE UNIVERSITY   (United States)

^b UNIVERSITY OF HONG KONG   (Hong Kong)

Author keywords

Caseins; Lactoferrin; Lactoperoxidase; Milk proteins; Whey proteins

Indexed keywords

CALCIUM PHOSPHATE; PRECIPITATION (CHEMICAL);

COLLOIDAL PARTICLE; FUNCTIONAL PROPERTIES; HEAT-STABLE PROTEINS; LACTOFERRIN; LACTOPEROXIDASE; MEMBRANE PROTEINS; MILK PROTEIN; STRUCTURAL-FUNCTIONAL; WHEY PROTEINS;

CASEIN;

EID: 84927792245     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9781118860588.ch16     Document Type: Chapter

References (136)

1. Abascal, D.M. and Gracia-Fadrique, J. (2009). Surface tension and foam stability of commercial calcium and sodium caseinates. Food Hydrocoll. 23:1848-1852.
2. Abd El-Salam, M.H. and El-Shibiny, S. (2012). Formation and potential uses of milk proteins as nano delivery vehicles for nutraceuticals: a review. Int. J. Dairy Technol. 65:13-21.
3. Anema, S.G., Pinderb, D.N., Hunterb, R.J., and Hemar, Y. (2006). Effects of storage temperature on the solubility of milk protein concentrate (MPC85). Food Hydrocoll. 20:386-393.
4. Aoki, T., Toyooka, K., and Kako, Y. (1985). Role of phosphate groups in the calcium sensitivity of αs2-casein. J. Dairy Sci. 68:1624-1629.
5. Avena-Bustillos, R.J. and Krochta, J.M. (1993). Water vapor permeability of caseinate-based edible films as affected by pH, calcium crosslinking ligand and lipid content. J. Food Sci. 58(4):904-907.
6. Baker, E.N. and Baker, H.M. (2005). Molecular structure, binding properties and dynamics of lactoferrin. Cell. Mol. Life Sci. 62:2531-2539.
7. Baldwin, A.J. (2010). Insolubility of milk powder products - a mini review. Dairy Sci. Technol. 90:169-179.
8. Belitz, H.-D., Grosch, W., and Schieberle, P. (2009). Food Chemistry (4th revised and extended edn). Heidelberg, Germany: Springer-Verlag. p. 502.
9. Bhaskar, G.V., Singh, H., and Blazey, N.D. (2001). Milk protein products and processes. Patent WO01/41578.
10. Brew, K. and Grobler, J.A. (1992). α-Lactalbumin. In: Fox, P.F. (ed) Advanced Dairy Chemistry-1: Proteins (2nd edn). London: Elsevier Applied Science Publishers. pp. 191-229.
11. Brew, K., Vanaman, T.C., and Hill, R.L. (1968). The role of α-lactalbumin and a protein in lactose synthetase: a unique mechanism for the control of a biological reaction. Biochem. 59:491-497.
12. Brignon, G., Ribadeau Dumas, B., Mercier, J.-C., Pelissier, J.-P., and Das, B.C. (1977). The complete amino acid sequence of bovine αS2-casein. FEBS Lett. 76:274-279.
13. Brunner, J.R. and Kester, J.J., (1982). Milk fat-globule membrane as possible origin of proteose peptone glycoproteins. J. Dairy Sci. 65:2241-2252.
14. Butler, J.E. (1969). Bovine immunoglobulins. A review. J. Dairy Sci. 52:1895-1907.
15. Carr, A.J. (2002). Monovalent salt enhances solubility of milk protein concentrate. Patent WO02/096208.
16. Carter, D.C. and Ho, J.X. (1994). Structure of serum albumin. Adv. Protein Chem. 45:153-203.
17. Cayot, P., Courhaudon J-L., and Lourient, D. (1991). Emulsifying properties of pure and mixed αs1- and β-casein fractions: effects of chemical glycosylation. J. Agric. Food Chem. 39:1369-1373.
18. Clare, D.A. and Swaisgood, H.E. (2000). Bioactive milk peptides: a prospectus. J. Dairy Sci. 83:1187-1195.
19. Considine, T., Patel, H.A., Anema, S.G., Singh, H., and Creamer, L.K. (2007). Interactions of milk proteins during heat and high hydrostatic pressure treatments: aReview. Innovative Food Sci. and Emerging Technol. 8:1-23.
20. Creamer, L.K., Richardson, T., and Parry, D.A.D. (1981). Secondary structures of bovine αs1- and β-casein in solution. Arch. Biochem. Biophys. 211:689-696.
21. Csapó-Kiss, Z.s., Stefler, J., Martin, T.G., Makray, S., Csapó, J. (1995). Composition of mares' colostrum and milk. Protein content, amino acid composition and contents of macro- and microelements. Int. Dairy J. 5:403-415.
22. Dalgleish, D.G. and Law, A.J.R. (1988). pH-induced dissociation of bovine casein micelles. Analysis of liberated caseins. J. Dairy Res. 55:529-38.
23. Dalgleish, D.G., Spagnuolo P.A., and Goff, H.D. (2004). A possible structure of the casein micelle based on high-resolution field-emission scanning electron microscopy. Int. Dairy J. 14: 1025-1031.
24. Damodaran, S. (1994). Structure-function relationship of food proteins. In: Hettiarachchy, N.S. and Ziegler, G.R. (eds) Protein Functionality in Food Systems. New York: Marcel Dekker. pp. 1-37.
25. de Kruif, C.G. (1999). Casein micelle interactions. Int. Dairy J. 9:183-188.
26. de Kruif, C.G. and Grinberg, V.Y. (2002). Micellization of β-casein. Colloids Surf. A: Physicochem. Eng. Asp. 210:183-190.
27. de Kruif, C.G. and Holt, C. (2003). Casein micelle structure, functions and interactions. In: Fox, P.F., and McSweeney, P.L.H. (eds) Advanced Dairy Chemistry, Volume 1: Proteins (3rd edn). New York: Kluwer Academic/Plenum Publishers. pp. 233-276.
28. de Kruif, C.G., Huppertz, T., Urban, V.S., and Petukhov, A.V. (2012). Casein micelles and their internal structure. Adv. Colloid and Interface Sci. 171-172:36-52.
29. DeVilbiss, E.D., Holsinger, V.H., Posati, L.P., and Pallansch, M.J. (1974). Properties of whey protein concentrates. Food Technol. 28(3):40-42, 46, 48.
30. de Wit, J.N. and van Hooydonk, A.C.M. (1996). Structure, functions and applications of lactoperoxidase in natural antimicrobial systems. Neth. Milk Dairy J. 50:227-244.
31. Dickinson, E. (2003). Interfacial, emulsifying and foaming properties of milk proteins. In: Fox, P.F. and McSweeney, P.L.H. (eds) Advanced Dairy Chemistry, Volume 1: Proteins (3rd edn). New York: Kluwer Academic/Plenum Publishing. pp. 1229-1260.
32. Dziuba, J. and Minkiewicz, P. (1996). Influence of glycosylation on micelle-stabilizing ability and biological properties of C-terminal fragments of cow's κ-casein. Int. Dairy J. 6:1017-1044.
33. Eigel, W.H., Butler, J.E., Ernstrom, C.A., Farrell Jr., H.M., Harwalkar, V.R., Jenness, R. and McWhitney, R. (1984). Nomenclature of proteins of cow's milk: fifth revision. J. Dairy Sci. 67:1599-1631.
34. Elfstranda, L., Lindmark-Manssonb, H., Paulssona, M., Nybergc, L., and Akesson, B. (2002). Immunoglobulins, growth factors and growth hormone in bovine colostrum and the effects of processing. Int. Dairy J. 12:879-887.
35. Farnaud S. and Evans, R.W. (2003). Lactoferrin-a multifunctional protein with antimicrobial properties. Mol. Immunol. 40:395-405.
36. Farrell Jr., H.M. (1988). Physical equilibria: proteins. In: Wong, N. (ed) Fundamentals of Dairy Chemistry (3rd edn). New York, NY: Van Nostrand. pp. 461-510.
37. Farrell Jr., H.M., Brown, E.M., Hoagland, P.D., and Malin, E.L. (2003). Higher order structures of caseins: a paradox. In: Fox, P.F. and McSweeney, P. (eds) Advanced Dairy Chemistry-1. Proteins. Part A (3rd edn). London, UK: Kluwer Academic. pp. 203-232.
38. Farrell Jr., H.M., Jimenez-Flores, R., Bleck, G.T., Brown, E.M., Butler, J.E., Creamer, L.K., Hicks, C.L., Hollar, C.M., Ng-Kwai-Hang, K.F., and Swaisgood, H.E. (2004). Nomenclature of the proteins of cows' milk-sixth revision. J. Dairy Sci. 87:1641-1674.
39. Fox, P.F. and Brodkorb, A. (2008). The casein micelle: historical aspects, current concepts and significance. Int. Dairy J. 18:677-684.
40. Fox, P.F. and McSweeney, P.L.H. (1998). Dairy Chemistry and Biochemistry. London: Blackie Academic & Professional.
41. Fox, P.F. and Mulvihill, D.M. (1983). Functional properties of caseins, caseinates and coprecipitates. In: International Dairy Federation, Brussels, Belgium (eds) I.D.F. Symposium: Physicochemical Aspects of Dehydrated Protein-Rich Milk Products. Helsingør, Denmark. pp. 188-259.
42. Gallagher, D.P., Cotter, P.F., and Mulvihill, D.M. (1997). Porcine milk protein: a review. Int. Dairy J. 7:99-118.
43. Gelamo, E.L., Silva, C.H., Imasat, H., and Tabak, M. (2002). Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modeling. Biochim. Biophys. Acta 1594:84-99.
44. Gelamo, E.L. and Tabak, M. (2000). Spectroscopic studies on the interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants. Spectrochim. Acta A Mol. Biomol. Spectrosc. 56:2255-2271.
45. Girardet, J.M. and Linden, G. (1996). PP3 component of bovine milk. A phosphorylated whey glycoprotein. J. Dairy Res. 63:333-350.
46. Gonzalez-Chavez, S.A., Arevalo-Gallegos, S., and Rascon-Cruz, Q. (2009). Lactoferrin: structure, function and applications. Int. J. Antimicrobial Agents 33:301.e1-301.e8.
47. Groves, M.L., Basch, J.J., and Gordon, W.G. (1963). Isolation, characterization and amino acid composition of a new crystalline protein, lactollin, from milk. Biochem. 2:814-817.
48. Guo, M.R., Fox, P.F., Flynn, A., and Kindstedt, P.S. (1996). Heat-induced modification of the functional properties of sodium caseinate. Int. Dairy J. 6:473-483.
49. Ha, E. and Zemel, M.B. (2003). Functional properties of whey, whey components, and essential amino acids: mechanisms underlying health benefits for active people. J. Nutr. Biochem. 14: 251-8.
50. Harmsen, M.C., Swart, P.J., de Béthune, M.P., Pauwels, R., de Clercq, E., Bauw, T., and Meijer, D.K.F. (1995). Antiviral effects of plasma and milk proteins: lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro. J. Infect Dis. 172:380-388.
51. Havea, P. (2006). Protein interactions in milk protein concentrate powders. Int. Dairy J. 16:415-422.
52. Holt, C. (1992). Structure and stability of bovine casein micelles. Adv. Protein Chem. 43:63-151.
53. Horne, D.S. and Banks, J. (2004). Rennet-induced coagulation of milk. In: Fox, P.F., McSweeney, P.L.H., Coagan, T.M., and Guinee, T. (eds) Cheese: Chemistry, Physics and Microbiology (Vol. 1). Oxford: Elsevier Applied Science Publishers. pp. 47-70.
54. Hsia, J.C., Wong, L.T., Tan, C.T., Er, S.S., Kharouba, S., Balaskas, E., Tinker D.O., and Feldhoff, R.C. (1984). Bovine serum albumin: characterization of a fatty acid binding site on the N-terminal peptic fragment using a new spin-label. Biochem. 23:5930-5932.
55. Huppertz, T. (2010). Foaming properties of milk: a review of the influence of composition and processing. Int. J. Dairy Technol. 63:477-488.
56. Imafidon, G.I., Farkye, N.Y., and Spanier, A.M. (1997). Isolation, purification, and alteration of some functional groups of major milk proteins. Crit. Rev. Food Sci. Nutr. 37:663-689.
57. Innocente, N., Corradini, C., Blecker C., and Paquot, M. (1998). Dynamic surface properties of proteose-peptone fraction of bovine milk. J. Dairy Sci. 81:1833-1839.
58. Janer, C., Pelaez, C., and Requena, T. (2004). Caseinomacropeptide and whey protein concentrate enhance Bifidobacterium lactis growth in milk. Food Chem. 86:263-267.
59. Kim, Y.A., Chism III, G.W., and Mangino, M.E. (1987). Determination of the beta-lactoglobulin, alpha-lactalbumin and bovine serum albumin of whey protein concentrates and their relationship to protein functionality. J. Food Sci. 52:124-127.
60. Kinsella, J.E. (1977). Functional properties of proteins in foods: a survey. Crit. Rev. Food Sci. Nutr. 7:219-280.
61. Kinsella, J.E. (1984). Milk proteins: physicochemical and functional properties. CRC Crit. Rev. Food Sci. Nutri. 21(3):197-262.
62. Kobylka, D. and Carraway, K.L. (1972). Proteins and glycoproteins of the milk fat globule membrane. Biochim. Biophys. Acta 288:282-295.
63. Kobylka, D. and Carraway, K.L. (1973). Proteolytic digestion of proteins of the milk fat globule membrane. Biochim. Biophys. Acta 307:133-140.
64. Korhonen, H., Marnila P., and Gill, H.S. (2000). Milk immunoglobulins and complement factors. British J. Nutr. 84(Suppl. 1):S75-S80.
65. Kuwajima, K., Ikeguchi, M., Sugawara, T., Hiraoka, Y., and Sugai, S. (1990). Kinetics of disulfide bond reduction in α-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond. Biochem. 29:8240-8249.
66. Law, A.J.R. and Leaver, J. (2000). Effect of pH on the thermal denaturation of whey proteins in milk. J. Agric. Food Chem. 48:672-679.
67. Lencki, R.W. (2007). Evidence for fibril-like structure in bovine casein micelles. J. Dairy Sci. 90: 75-89.
68. Levay, P.F. and Viljoen, M. (1995). Lactoferrin: a general review. Haematologica 80:252-267.
69. Liao, S.Y. and Mangino, M.E. (1987). Characterization of the composition, physicochemical and functional properties of acid whey protein concentrates. J. Food Sci. 52:1033-1037.
70. Li-Ghan, E., Kummer, A., Losso, J.N., Kitts, D.D., and Nakai, S. (1995). Stability of bovine immunoglobulins to thermal treatment and processing. Food Res. Int. 28:9-16.
71. Madureira, A.R., Pereira, C.I., Gomes, A.M.P., Pintado, M.E., and Malcata, F.X. (2007). Bovine whey proteins - Overview on their main biological properties. Food Res. Int. 40:1197-1211.
72. MAF Quality Management (1996). Physical Properties of Dairy Products (3rd edn). New Zealand: Ministry of Agriculture. p. 47.
73. Mangino, M. (2007). Whey protein concentrates. http://class.fst.ohio-state.edu/FST822/lecturesab/WPC.htm (accessed May 3, 2013).
74. Markus, C.R., Olivier, B., and deHaan, E.H.F. (2002). Whey protein rich in α-lactalbumin increases the ratio of plasma tryptophan to the sum of the other large neutral amino acids and improves cognitive performance in stress-vulnerable subjects. Am. J. Clinical Nutr. 75:1051-1056.
75. Marshall, K. (2004). Therapeutic applications of whey protein. Alternative Med. Rev. 9:136-156.
76. Marushige, Y. and Mangino, M.E. (1989). Factors important to the acceptability of gelled whey protein concentrates. Cultured Dairy Prod. J. 24(3):9, 11-13.
77. Mather, I.H. and Keenan, T.W. (1975). Studies on the structure of milk fat globule membrane. J. Membr. Biol. 21:65-85.
78. McCann, K.B., Shiell, B.J., Michalski, W.P., Lee, A., Wan, J., Roginski, H., and Coventry, M.J. (2005). Isolation and characterization of antibacterial peptides derived from the f(164-207) region of bovine αs2-casein. Int. Dairy J. 15:133-143.
79. McHugh, T.B. and Krochta, J.M. (1994). Milk-protein based edible films and coatings. Food Technol. 97-103.
80. McIntosh, G.H., Royle, P.J., Le Leu, R.K., Regester, G.O., Johnson, M.A., Grinsted, R.L., Kenward, R.S., and Smithers, G.W. (1998). Whey proteins as functional foods ingredients. Int. Dairy J. 8:425-434.
81. McKee, M.M. and Sills, M.A. (2003). Disinfection and cleaning system for contact lenses. US Patent No. 0118472 A1.
82. McMahon, D.J. and McManus, W.R. (1998). Rethinking casein micelle structure using electron microscopy. J. Dairy Sci. 81:2985-2993.
83. McMahon, D.J. and Oommen B.S. (2008). Supramolecular structure of the casein micelle. J. Dairy Sci. 91:1709-1721.
84. Mehra, R., Marnila P., and Korhonen, H. (2006). Milk immunoglobulins for health promotion. Int. Dairy J. 16:1262-1271.
85. Migliore-Samour, D. and Jollès, P. (1988). Casein, a pro-hormone with an immunomodulating role for the newborn? Experimentia 44:188-193.
86. Mills, S., Ross, R.P., Hill, C., Fitzgerald, G.F., and Stanton, C. (2011). Milk intelligence: mining milk for bioactive substances associated with human health. Int. Dairy J. 21:377-401.
87. Mollè, D., Jean, K., and Guyomarch, F. (2006). Chymosin sensitivity of the heat-induced serum protein aggregates isolated from skim milk. Int. Dairy J. 16:1435-1441.
88. Mollè, D. and Leonil, L. (1995). Heterogeneity of the bovine κ-casein caseinomacropeptide, resolved by liquid chromatography on-line with electrospray ionization mass spectrometry. J. Chromatogr. A 708:223-230.
89. Morr, C.V. (1979). Functionality of whey protein products. N. Z. J. Dairy Sci. Technol. 14:185-194, 201-204.
90. Murphy, J.M. and Fox, P.F. (1991). Fractionation of sodium caseinate by ultrafiltration. Food Chem. 39:27-38.
91. Murrieta-Pazos, I., Gaiani, C., Galet, L., Cuq, B., Desobry, S., and Scher, J. (2011). Comparative study of particle structure evolution during water sorption: skim and whole milk powders. Colloids Surf. B: Biointerfaces 87:1-10.
92. Nair, K.S., Schwartz, R.G., and Welle, S. (1992). Leucine as a regulator of whole body and skeletal muscle protein metabolism in humans. Am. J. Physiol. - Endocrinology and Metabolism 263:E928-E934.
93. Naot, D., Palmano K., and Cornish, J. (2012). Lactoferrin - A Potential Anabolic Intervention in Osteoporosis, Osteoporosis, PhD. Yannis Dionyssiotis (ed.), In Tech, Available from: http://www.intechopen.com/books/osteoporosis/lactoferrin-a-potential-anabolic-interventioninosteoporosis (accessed March 15:2013).
94. O'Connell, J.E. and Fox, P.F. (2000). The two-stage coagulation of milk proteins in the minimum of the heat coagulation time-pH profile of milk: effect of casein micelle size. J. Dairy Sci. 83: 378-386.
95. O'Connell, J.E., Kelly, A.L., Fox, P.F., and de Kruif, K.G. (2001). Mechanism for the ethanoldependent heat-induced dissociation of casein micelles. J. Agric. Food Chem. 49:4424-4428.
96. Pan, Y., Lee, A., Wan, J., Coventry, M.J., Michalski, W.P., Shiell, B, and Roginski, H. (2006). Antiviral properties of milk proteins and peptides. Int. Dairy J. 16:1252-1261.
97. Patton, S. and Keenan, T.W. (1975). The milk fat globule membrane. Biochim. Biophys. Acta 415:273-309.
98. Pedersen, L.R.L., Hansted, J.G., Nielsen, S.B., Petersen, T.E., Sørensen, U.S., Otzen, D., and Sørensen E.S. (2012). Proteolytic activation of proteose peptone component 3 by release of a C-terminal peptide with antibacterial properties. J. Dairy Sci. 95:2819-2829.
99. Pierce, A., Colavizza, D., Benaissa, M., Maes, P., Tartar, A., Montreuil, J., and Spik, G. (1991). Molecular cloning and sequence analysis of bovine lactotransferrin. Eur. J. Biochem. 196: 177-184.
100. Poulsen, O.M. (1988). Enzyme-containing bactericidal composition, and dental and wound treatment preparations comprising this composition. Australian Patent No. AU 1987081750 A; (also, WIPO Patent No. WO 1988002600, April 22, 1988.
101. Rammer P., Groth-Pedersen, L., Kirkegaard, T., Daugaard, M., Rytter, A., Szyniarowski, P., Høyer-Hansen, M., Povlsen, L.K., Nylandsted, J., Larsen, J.E., and Jäättelä, M. (2010). BAMLET activates a lysosomal cell death program in cancer cells. Mol. Cancer Therapeutics 9:24-32.
102. Reed, R.G., Feldhoff, R.C., Clute O.L., and Peters Jr., T. (1975). Fragments of bovine serum albumin produced by limited proteolysis. Conformation and ligand binding. Biochem. 14:4578-4583.
103. Reiter, B. and Harnulv, G. (1984). Lactoperoxidase antibacterial system: natural occurrence, biological function and practical applications. J. Food Prot. 47:724-732.
104. Rieu, I., Balage, M., and Sornet, C. (2007). Increased availability of leucine with leucine-rich whey proteins improves postprandial muscle protein synthesis in ageing rats. Nutrition 23: 323-31.
105. Rittmanic, S. (2006). U.S. Whey proteins in ready-to-drink beverages. U.S. Dairy Export Council Arlington, VA.
106. Rollema, H.S. (1992). Casein association and micelle formation. In: Fox, P.F. (ed) Advanced Dairy Chemistry Volume 1: Proteins (2nd edn). Barking, UK: Elvsevier. pp. 111-140.
107. Saito, T. and Itoh, T. (1992). Variations and distributions of O-glycosidically linked sugar chains in bovine κ-casein. J. Dairy Sci. 75:1768-1774.
108. Schmidt, R.H. (1978). The effect of heat treatment on aggregation and gelation of peanut/milk protein blends. Cereal Chem. 55:58-65.
109. Schmidt, D.G. (1980). Colloidal aspects of the caseins. Neth. Milk Dairy J. 34:42-64.
110. Schokker, E.P., Church, J.S., Mata, J.P., Gilbert, E.P., Puvanenthiran, A., and Udabage, P. (2011). Reconstitution properties of micellar casein powder: effects of composition and storage. Int. Dairy J. 21:877-886.
111. Schuck, P., Piot, M., Mejean, S., Legraet, Y., Fauquant, J., Brule, G., and Maubois, J.L. (1994). Spray-drying of native phosphocaseinate obtained by membrane microfiltration. Lait 74: 375-388.
112. Shimada, K. and Cheftel, J.C. (1989). Sulfhydryl group/disulfide bond Interchange reactions during heat-induced gelation of whey protein isolate. J. Agric. Food Chem. 37:161-168.
113. Singh, H. (2011). Aspects of milk-protein-stabilized emulsions. Food Hydrocoll. 25:1938-1944.
114. Slattery C.W. and Evard, R. (1973). A model for the formation and structure of casein micelles from subunits of variable composition. Biochim. Biophys. Acta 17:529-38.
115. Sørensen, E.S. and Petersen, E.T. (1993). Purification and characterization of three proteins isolated from the proteose-peptone fraction of bovine milk. J. Dairy Res. 60:189-197.
116. Stănciuc, N. and Rapeanu, G. (2010). An overview of bovine α-lactalbumin structure and functionality. Innov. Rom. Food Biotechnol. 34:82-93.
117. Steijns J.M. and van Hooijdonk, A.C.M. (2000). Occurrence, structure, biochemical properties and technological characteristics of lactoferrin. Br. J. Nutr. 84(Suppl. 1):S11-S17.
118. Svanborg, C., Agerstam, H., Aronson, A., Bjerkvig R., and Duringer, C. (2003). HAMLET kills tumor cells by an apoptosis-like mechanism-cellular, molecular, and therapeutic aspects. Adv. Cancer Res. 88:1-29.
119. Swaisgood, H.E. (1995). Protein and amino acid composition of bovine milk. In: Jensen, R.G. (ed) Handbook of Milk Composition. San Diego: Academic Press. pp. 464-472.
120. Swaisgood, H.E. (2003). Chemistry of caseins. In: Fox, P.F. and McSweeney, P.L.H. (ed.). Advanced Dairy Chemistry. Vol. 1: Proteins (3rd edn). New York, NY: Kluwer. pp. 139-202.
121. Tanford, C., Bunville, L.G., and Nozaki, Y. (1959). The reversible transformation of β-lactoglobulin at pH 7.5. J. Am. Chem. Soc. 81:4032-4036.
122. Tenovuo, J. (2002). Clinical applications of antimicrobial host proteins lactoperoxidase, lysozyme and lactoferrin in xerostomia: efficacy and safety. Oral Diseases 8:23-29.
123. Tomita, M., Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., and Kawase, K. (1992). Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin. J. Dairy Sci. 74:4137-4142.
124. Totosaus, A., Montejano, J.G., Salazar, J.A., and Guerrero, I. (2002). A review of physical and chemical protein-gel induction. Int. J. Food Sci. Technol. 37:589-601.
125. Treece, J.M., Sheinson, R.S., and McMeekin, T.L. (1964). The solubilities of β-lactoglobulins A, B, and AB. Arch. Biochem. Biophy. 108:99-108.
126. USDA Nutrient Data. Nutrient data for Milk, nonfat, fluid, without added vitamin A and vitamin D. http://www.ars.usda.gov/ba/bhnrc/ndl (accessed Nov.12, 2012).
127. USDEC (2006). Milk Protein Ingredients. U.S. Dairy Export Council. Arlington, VA.
128. Valente-Mesquita, V.L., Botelho, M.M., and Ferreira, S.T. (1998). Pressure-induced subunit dissociation and unfolding of β-lactoglobulin. Biophys. J. 75:471-476.
129. van Calcar, S.C. and Ney, D.M. (2012). Food products made with glycomacropeptide, a lowphenylalanine whey protein, provide a new alternative to amino acid-based medical foods for nutrition management of phenylketonuria. J. Acad. Nutr. Diet. 112:1201-1210.
130. Voutsinas, L.P., Nakai, S., and Harwalkar, V.R. (1983). Relationships between protein hydrophobicity and thermal functional Properties of Food Proteins. Can. Inst. Food Sci. Technol. J. 16: 185-190.
131. Walstra, P. (1990). On the stability of casein micelles. J. Dairy Sci. 73:1965-1979.
132. Walstra, P. (1999). Casein sub-micelles: do they exist? Int. Dairy J. 9:189-192.
133. Waugh, D.F. (1958). The interaction of αs, β- and κ-caseins in micelle formation. Faraday Society Discuss 25:186-192.
134. Wetzel, R., Becker, M., Behlke, J., Billwitz, H., Böhm, H., Ebert, B., Hamann, H., Krumbiegel, J., and Lassmann, G. (1980). Temperature behavior of human serum albumin. Eur. J. Biochem. 104:469-478.
135. Zadow, J.G. (1993). Alcohol-mediated temperature-induced reversible dissociation of the casein micelle in milk. Aust. J. Dairy Technol. 48:78-81.
136. Zittle, C.A. and Walter, M. (1963). Stabilization of β-CN by κ-CN against precipitation by calcium chloride. J. Dairy Sci. 24:1189-1191.