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Heat stability of milk: influence of denaturable proteins and detergents on pH sensitivity

Published online by Cambridge University Press:  01 June 2009

Patrick F. Fox  and
Catherine M. Hearn
Patrick F. Fox
Affiliation:
Department of Food Chemistry, University College, Cork, Irish Republic
Catherine M. Hearn
Affiliation:
Department of Food Chemistry, University College, Cork, Irish Republic
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Summary

α-Lactalbumin and SDS in addition to β-lactoglobulin introduced pH sensitivity to the heat stability–pH curve of serum protein free casein micelles particularly by increasing stability in the pH range 6·4–6·7. Bovine serum albumin, ovalbumin and lysozyme caused marked destabilization of milk and casein micelle suspensions throughout the pH range 6·4–7·4. Tetramethyl ammonium bromide caused destabilization of milk at pH values > 7·0, but had no effect in the region of maximum stability while the non-ionic detergents Triton X-100 and Tween 80 had no effect on heat stability.

Type
Original Articles
Information
Journal of Dairy Research , Volume 45 , Issue 2 , June 1978 , pp. 159 - 172
Copyright
Copyright © Proprietors of Journal of Dairy Research 1978

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