Dairy Microbiology Handbook: The Microbiology of Milk and by Richard K. Robinson

By Richard K. Robinson

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Additional resources for Dairy Microbiology Handbook: The Microbiology of Milk and Milk Products (3rd Edition)

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24, 143-147. Harper, W. , and Hall, C. W. (1976) Processing-induced changes. Chapter 13 in Duirv Technology and Engineering, AVI Press, Westport. CT. Hillier, R. , and Lyster, R. L. J. (1979) J. Dairy Rex, 46,95-102. Holt, C. ( 1992) Structure and stability of bovine casein micelles. In Advance5 in Protein Chemistry, C. B. ,4finsen, J. D. E. D. Sall, F. K. Richards, and D. S. , Academic Press, New York, pp. 63-1 5 1. Horne, D. S. (1998) Int. , 8,171-177. , Goddard, P. , Kitchen, B. , and Masters, C.

1985; Dalgleish and Law, 1988). 5 (Dalgleish and Law, 1988). 6) is approached. , 1985). , 1996). , 1996). The exact nature of the casein paiticles that exist in acidified milk is uncertain. 3, most of the CCP in the micelles is solubilized, the native charges on individual caseins are reduced, and the ionic strength of the solution increases. It is expected that the forces responsible for the integrity of these "micelle-like" CCP-depleted casein particles would be considerably different from those in native micelles even if the average hydrcjdynamic diameter appears to be largely unchanged.

However, at high temperatures and fast heating rates, all whey proteins begin to unfold in a short period of time, thus presenting more opportunity for unfolded monomeric P-lactoglobulin to self-aggregate, which consequently is likely to associate with the casein micelles less efficiently. Casein micelles are very stable at high temperatures. although changes in zeta potential, size, and hydration of micelles, as well as some association-dissociation reactions, do occur at severe heating temperatures (Fox, 1981; Singh, 1988;Singh and Creamer, 1992).

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