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The reactivation of milk alkaline phosphatase after heat treatment

Published online by Cambridge University Press:  01 June 2009

R. L. J. Lyster  and
R. Aschaffenburg
R. L. J. Lyster
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading
R. Aschaffenburg
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading
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Summary

A simple system was developed, consisting of a solution of β-glycerophosphate, β-lactoglobulin and magnesium ions, in which alkaline phosphatase isolated from milk became strongly reactivated following heat treatment for 45 sec in boiling water. From 10 to 30% of the original enzyme activity reappeared after incubation at 37°C. Variations in the components of the system, and factors affecting it, were studied. Salts of Hg, Zn and Cd inhibited reactivation at low concentrations.

Milk which, after the same heat treatment, became reactivated to a much smaller extent (about 1%), was found to contain a dialysable, heat labile inhibitor whose presence is thought to be largely responsible for the low level of reactivation, though other factors, e.g. the suboptimal concentration of phosphate esters must be considered as contributory causes.

Milk contains also a non-dialysable, heat stable activator of the reactivation process, capable of replacing β-lactoglobulin in the simple system and active at very low concentration, e.g. 0·2% (v/v).

Type
Original Articles
Information
Journal of Dairy Research , Volume 29 , Issue 1 , February 1962 , pp. 21 - 35
Copyright
Copyright © Proprietors of Journal of Dairy Research 1962

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References

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