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Influence of aggregation on the susceptibility of casein to proteolysis

Published online by Cambridge University Press:  01 June 2009

P. F. Fox
P. F. Fox
Affiliation:
National Dairy Research Centre, The Agricultural Institute, Fermoy, Co. Cork, Irish Republic
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Summary

The susceptibility of the casein in milk to proteolysis was shown to be greatly influenced by its state of aggregation. In normal milk, where the casein is largely in micellar form, the αs1- and β-caseins are almost inaccessible to proteolysis. On removal of the colloidal phosphate, the casein micelles disintegrate, rendering the components, especially the αs1-casein, accessible to proteolysis. The role of colloidal calcium phosphate in the casein micelle is believed to be that of a non-specific aggregating agent which can be effectively replaced by calcium. Dissolved colloidal phosphate can be effectively reformed by elevation of the pH of colloidal phosphate-free (CPF) milk before equilibrium dialysis. Addition of κ-casein to CPF milk also causes aggregation of the component caseins but the micelles formed are smaller than those of normal milk.

The behaviour of micellar β-casein differs considerably from that of micellar αs1-casein. The evidence suggests that part of the β-casein freely dissociates either outside or within the micelle when the temperature is reduced. The temperature dependence of the susceptibility of β-casein to proteolysis was similar in skim-milk and in solutions of sodium caseinate, and increased as the temperature was reduced. αs1-Casein was quite resistant to proteolysis in normal milk but became susceptible when the micelle structure was disrupted on removal of colloidal phosphate.

It is concluded that limited proteolysis may prove a valuable technique in the study of casein micelle structure.

Type
Original Articles
Information
Journal of Dairy Research , Volume 37 , Issue 2 , June 1970 , pp. 173 - 180
Copyright
Copyright © Proprietors of Journal of Dairy Research 1970

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