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 |
|---|---|
| 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 |
Cite this
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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 journal › Article › Research › peer-review
TY - JOUR
T1 - Heat-induced interaction of βMactoglobulin and k-casein
AU - McKenzie, G. H.
AU - Norton, R. S.
AU - Sawyer, W. H.
PY - 1971
Y1 - 1971
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84974489139&partnerID=8YFLogxK
U2 - 10.1017/S0022029900019476
DO - 10.1017/S0022029900019476
M3 - Article
VL - 38
SP - 343
EP - 351
JO - Journal of Dairy Research
JF - Journal of Dairy Research
SN - 0022-0299
IS - 3
ER -