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The specificity for κ-casein as the stabilizer of αs-casein and β-casein. I. Replacement of κ-casein by other proteins

Published online by Cambridge University Press:  01 June 2009

Margaret L. Green
Margaret L. Green
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading, RG2 9AT
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Summary

The specificity of the interaction between κ-casein, αs-casein and β-casein which forms the basis of micelle stabilization was studied by investigating the extent to which κ-casein could be replaced by other proteins. Of those tested, only gelatin replaced κ-casein and even it was only 2·5% (w/v) as effective and required a long pre-incubation period. The micelles formed by each of κ-casein and gelatin with αs-casein and Ca2+ were of a similar size to the casein—Ca complexes which compose natural micelles. Gelatin also formed complexes with αs- and with β-casein at 30°C in the absence of CaCl2. Evidence was obtained that the interactions between gelatin and the caseins had a much stronger ionic component than had those between κ-casein and the other caseins. It was concluded that the interactions between κ-casein and αs- and β-caseins which lead to micelle formation are highly specific and probably involve definite sites in each molecule.

Type
Original Articles
Information
Journal of Dairy Research , Volume 38 , Issue 1 , February 1971 , pp. 9 - 23
Copyright
Copyright © Proprietors of Journal of Dairy Research 1971

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