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 language | English |
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Pages (from-to) | 343-351 |
Number of pages | 9 |
Journal | Journal of Dairy Research |
Volume | 38 |
Issue number | 3 |
DOIs | |
Publication status | Published - 1971 |
Externally published | Yes |