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Electrophoretic mobility 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, MK44 1LQ
John Dickson
Affiliation:
Unilever Research Laboratory, Colworth House, Sharnbrook, Bedford, MK44 1LQ
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Summary

A simplified moving boundary electrophoresis technique has been developed for the measurement of the electrophoretic mobility of casein micelles. The zeta potentials of casein micelles from different skim-milk samples were calculated using Henry's equation and shown to decrease with decrease in pH between pH 6.9 and 5.3 and to increase with increase in temperature between 10 and 45 °C. Neither severe heat treatment (up to 135 °C for 51 min) nor centrifugal fractionation of micelles into different micelle size ranges had any significant effect on zeta potential. The ionic composition of the serum phase has been shown to be extremely important in determining the electrophoretic mobility. Casein micelles electrophoresed through milk ultrafiltrate consistently gave a lower mobilities than the same micelles centrifuged through milk centrifugate. The results are discussed in relation to present theories of casein micelle structure; these theories do not accommodate all of the observations.

Type
Original Articles
Information
Journal of Dairy Research , Volume 46 , Issue 3 , July 1979 , pp. 441 - 451
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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