Heat-induced interaction of βMactoglobulin and k-casein

G. H. McKenzie, R. S. Norton, W. H. Sawyer

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Abstract

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

Original languageEnglish
Pages (from-to)343-351
Number of pages9
JournalJournal of Dairy Research
Volume38
Issue number3
DOIs
Publication statusPublished - 1971
Externally publishedYes

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