Dephosphorylation of αS- and κ-Caseins and Its Effect on Micelle Stability in the κ-αS-Casein System
Open Access
- 1 August 1963
- journal article
- research article
- Published by American Dairy Science Association in Journal of Dairy Science
- Vol. 46 (8) , 764-767
- https://doi.org/10.3168/jds.s0022-0302(63)89145-6
Abstract
Enzymatic dephosphorylation of [alpha]s - and [kappa]-caseins does not impair the formation of a stoichiometric complex of these proteins. In the presence of Ca ions, dephosphorylated [alpha]s-casein is only slightly stabilized by [kappa] -casein against precipitation; whereas dephosphorylation of [kappa]-casein alone yields [alpha]s - [kappa]-casein micelles which are stabile against Ca ion precipitation. Esterified calcium-phosphate linkages are formed among [alpha]s - [kappa] -casein complexes (in the absence of Ca) readily form indicating that the formation of H bonds and interaction of abundant non-polar side chains are responsible for complex formation.This publication has 12 references indexed in Scilit:
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