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The primary phase of rennin action in heat-sterilized milk

Published online by Cambridge University Press:  01 June 2009

E. J. Hindle  and
J. V. Wheelock
E. J. Hindle
Affiliation:
School of Biological Sciences, University of Bradford, Bradford 7
J. V. Wheelock
Affiliation:
School of Biological Sciences, University of Bradford, Bradford 7
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Summary

The action of rennin in milk subjected to the ultra-high-temperature heat sterilization process has been studied. The primary phase of rennin action, as determined by the release of peptides soluble in trichloroacetic acid, was partially inhibited as a result of the heat treatment. This was largely due to a reduction in the release of non-carbohydrate-containing peptides from κ-casein. It is suggested that when whole milk is heated the formation of a complex between β-lactoglobulin and κ-casein proceeds more readily with the species of κ-casein which lacks carbohydrate. Evidence is presented which shows that there may be more than one type of carbohydrate moiety attached to κ-casein.

Type
Original Articles
Information
Journal of Dairy Research , Volume 37 , Issue 3 , October 1970 , pp. 389 - 396
Copyright
Copyright © Proprietors of Journal of Dairy Research 1970

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