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The determination of the zeta potential of casein micelles

Published online by Cambridge University Press:  01 June 2009

Donald F. Darling  and
John Dickson
Donald F. Darling
Affiliation:
Unilever Research Laboratory, Colworth House, Sharnbrook, Bedford
John Dickson
Affiliation:
Unilever Research Laboratory, Colworth House, Sharnbrook, Bedford
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Summary

The principle of moving boundary electrophoresis has been employed for the measurement of the electrophoretic mobility and subsequent calculation of zeta potential of bovine casein micelles. The zeta potential of casein micelles was observed to increase with increase in temperature (from 10 to 50 °C) and to decrease with decrease in pH. Heat treatment of milk between 90 °C/30 min and 135 °C/50 min had no significant effect on zeta potential. The zeta potential of casein micelles during rennet action decreases until all the κ-casein has been cleaved by the enzyme.

The results of this study indicate that electrostatic interactions alone are not sufficient for an understanding of the absolute stability of casein micelles.

Type
Section D. Casein Micelles
Information
Journal of Dairy Research , Volume 46 , Issue 2: Symposium on the Physics and Chemistry of Milk Proteins , April 1979 , pp. 329 - 332
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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References

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