Heat-induced interaction of βMactoglobulin and k-casein

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

Research output: Contribution to journalArticleResearchpeer-review

36 Citations (Scopus)

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

Cite this

McKenzie, G. H. ; Norton, R. S. ; Sawyer, W. H. / Heat-induced interaction of βMactoglobulin and k-casein. In: Journal of Dairy Research. 1971 ; Vol. 38, No. 3. pp. 343-351.
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Heat-induced interaction of βMactoglobulin and k-casein. / McKenzie, G. H.; Norton, R. S.; Sawyer, W. H.

In: Journal of Dairy Research, Vol. 38, No. 3, 1971, p. 343-351.

Research output: Contribution to journalArticleResearchpeer-review

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T1 - Heat-induced interaction of βMactoglobulin and k-casein

AU - McKenzie, G. H.

AU - Norton, R. S.

AU - Sawyer, W. H.

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