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Dephosphorylation of bovine casein by milk alkaline phosphatase

Published online by Cambridge University Press:  01 June 2009

D. Lorient  and
G. Linden
D. Lorient
Affiliation:
Service de Biochimie Appliquée, Université de Nancy 1, C.O. 140 F.54037 Nancy, France
G. Linden
Affiliation:
Service de Biochimie Appliquée, Université de Nancy 1, C.O. 140 F.54037 Nancy, France
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Summary

The pH of optimum activity of alkaline phosphatase from cow's milk depended on the substrate, being 10·1 for p-nitrophenylphosphate, 8·6 for phosphoserine, 8·0 for phosvitin and 6·8 for casein. Individual casein components were dephosphorylated more rapidly than mixtures of αs- and β-caseins or of αs-, β- and κ-caseins and micellar casein. Mixtures of 2 components involving κ-casein were more readily dephosphorylated than αs- and β-casein mixtures. At pH 6·8, lactose, whey proteins and phosphate ions had an inhibitory effect. β-Lactoglobulin had an inhibitory effect only when the pH of the reaction was lower than the optimum pH value of the enzyme. Mg2+ and Zn2+ were not inhibitory. The optimum conditions for dephosphorylation of casein are described.

Type
Research Article
Information
Journal of Dairy Research , Volume 43 , Issue 1 , February 1976 , pp. 19 - 26
Copyright
Copyright © Proprietors of Journal of Dairy Research 1976

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