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Reformation of casein particles from alkaline-disrupted casein micelles

Published online by Cambridge University Press:  29 January 2008

Thom Huppertz ,
Betsy Vaia  and
Mary A Smiddy
Thom Huppertz*
Affiliation:
Department of Food and Nutritional Sciences, University College Cork, Cork, Ireland
Betsy Vaia
Affiliation:
Department of Food and Nutritional Sciences, University College Cork, Cork, Ireland Hochschule Wadenswil, Wadenswil, Switzerland
Mary A Smiddy
Affiliation:
Department of Food and Nutritional Sciences, University College Cork, Cork, Ireland
*
*For correspondence; e-mail: thom.huppertz@nizo.nl
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Abstract

In this study, the properties of casein particles reformed from alkaline disrupted casein micelles were studied. For this purpose, micelles were disrupted completely by increasing milk pH to 10·0, and subsequently reformed by decreasing milk pH to 6·6. Reformed casein particles were smaller than native micelles and had a slightly lower zeta-potential. Levels of ionic and serum calcium, as well as rennet coagulation time did not differ between milk containing native micelles or reformed casein particles. Ethanol stability and heat stability, >pH 7·0, were lower for reformed casein particles than native micelles. Differences in heat stability, ethanol stability and zeta-potential can be explained in terms of the influence of increased concentrations of sodium and chloride ions in milk containing reformed casein particles. Hence, these results indicate that, if performed in a controlled manner, casein particles with properties closely similar to those of native micelles can be reformed from alkaline disrupted casein micelles.

Keywords

Milkcasein micellealkaline disruptionsolvent quality
Type
Research Article
Information
Journal of Dairy Research , Volume 75 , Issue 1 , February 2008 , pp. 44 - 47
Copyright
Copyright © Proprietors of Journal of Dairy Research 2008

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