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Physico-chemical properties of casein micelles reformed from urea-treated milk

Published online by Cambridge University Press:  01 June 2009

T. C. A. McGann  and
P. F. Fox
T. C. A. McGann
Affiliation:
National Dairy Research Centre, The Agricultural Institute, Fermoy, Co. Cork, Irish Republic
P. F. Fox
Affiliation:
Department of Dairy and Food Chemistry, University College, Cork, Irish Republic
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Summary

Micelles reconstituted from urea-treated milk by exhaustive dialysis against bulk milk were similar to native micelles with respect to colloidal phosphate: casein ratio, ethanol stability, heat stability and susceptibility to first-stage rennin action. Reconstituted micelles were considerably smaller than native micelles as indicated by turbidity, sedimentation and viscosity, had shorter second-stage rennet coagulation times, were unstable to [Ca2+] > 20 mM and had reduced base-binding capacity. It is suggested that the induced Ca sensitivity is due to unfavourable alterations in the micellar κ-casein coat arising from the decrease in average micelle size and can be offset by increasing the κ-casein complement of the system or by increasing the degree of aggregation by slowly raising the [Ca2+] level.

Type
Research Article
Information
Journal of Dairy Research , Volume 41 , Issue 1 , February 1974 , pp. 45 - 53
Copyright
Copyright © Proprietors of Journal of Dairy Research 1974

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