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The formation of γ-caseins during cooling of raw milk

Published online by Cambridge University Press:  01 June 2009

Ernst H. Reimerdes
Affiliation:
Institute for Chemistry, Federal Dairy Research Centre, D 2300 Kiel, Federal Republic of Germany
Erika Herlitz
Affiliation:
Institute for Chemistry, Federal Dairy Research Centre, D 2300 Kiel, Federal Republic of Germany

Summary

It has been shown that there is a time-dependent transfer of β-casein and the milk serine proteinase system from micelles to milk serum with change of temperature from 38 to 4 °C. It has been established that the γ-caseins can be formed by proteolytic degradation of β-casein. By a simple extraction technique, the very hydrophobic γ-casein fraction was separated from stored milks (26 and 4 °C) and estimated quantitatively. The results showed that the proteolytic degradation of β-casein is faster at 4 °C than at room temperature and this can be explained by the immobilization of enzyme and substrate at the micelle surface at higher temperatures (26 °C).

The results indicate that irreversible changes during cooling for short periods do not cause problems in milk processing, but the formation of γ-caseins and phosphopeptides may influence the technological properties of raw milk stored for more than 48 h.

Type
Section B. Milk Proteins: Comparative Aspects, and the Study of some of the Minor Caseins
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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