Effect of low-temperature storage on the heat-induced complex of micellar casein with beta -lactoglobulin

Dziuba, J.

Zeszyty Naukowe Akademii Rolniczo Technicznej w Olsztynie, Technologia Zywnosci 16: 111-119

1981


Accession: 000868054

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Abstract
In continuation of earlier work [DSA 40, 946], modified casein containing 24.9% nitrated tyrosine residues was prepared by the method of Sokolovski et al. [Biochemistry (1966) 5 (11) 3582]. Solutions of micellar modified or unmodified casein containing 2.5% casein and 0.4% beta -lactoglobulin, without or with heating at 85 deg C for 15 s, were examined directly or after storage at 2 deg C for 5 days for glycopeptide liberation by crystalline chymosin at 9 deg C for 2 h. This incubation had been established to complete the 1st order phase of chymosin action. Tabulated and graphically presented results showed no difference between any of the variants in amounts of liberated glycopeptides or their N-acetylneuraminic acid contents. Therefore beta -lactoglobulin does not dissociate from the casein/ beta -lactoglobulin complex under low-temp. conditions under which hydrophobic interactions cease to take place.