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Heat-induced interaction of β-lactoglobulin and κ-casein

Published online by Cambridge University Press:  01 June 2009

G. H. McKenzie ,
R. S. Norton  and
W. H. Sawyer
G. H. McKenzie
Affiliation:
Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria 3052, Australia
R. S. Norton
Affiliation:
Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria 3052, Australia
W. H. Sawyer
Affiliation:
Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria 3052, Australia
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Summary

The interaction of β-lactoglobulin and κ-casein at high temperature was studied polarimetrically. The rate of interaction was related to the genetic variant of β-lactoglobulin present. β-Lactoglobulin B, whose thermodenaturation was faster than that of A variant, interacted more rapidly with κ-casein than did the A variant. Velocity sedimentation studies indicated that characteristics of the complex were determined more by the β-lactoglobulin than by the κ-casein. The presence of κ-casein during the thermodenaturation of β-lactoglobulin appeared to prevent the aggregation of β-lactoglobulin from proceeding to completion, the κ-casein complexing with intermediate species and restricting the aggregation process.

Type
Original Articles
Information
Journal of Dairy Research , Volume 38 , Issue 3 , October 1971 , pp. 343 - 351
Copyright
Copyright © Proprietors of Journal of Dairy Research 1971

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References

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