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Serological studies on heat-induced interactions of α-lactalbumin and milk proteins

Published online by Cambridge University Press:  01 June 2009

A. Baer ,
M. Oroz  and
B. Blanc
A. Baer
Affiliation:
Federal Dairy Research Institute, CH-3097 Liebefeld-Bern, Switzerland
M. Oroz
Affiliation:
Federal Dairy Research Institute, CH-3097 Liebefeld-Bern, Switzerland
B. Blanc
Affiliation:
Federal Dairy Research Institute, CH-3097 Liebefeld-Bern, Switzerland
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Summary

The heat denaturation of α-lactalbumin (α-la) in NaCl and KCl solutions, milk ultrafiltrate and milk was studied using the method of micro complement fixation. It was established that this protein was very resistant to heat denaturation and that it was more stable in milk ultrafiltrate than in the other media studied at temperatures up to 70 °C. Of the various milk proteins added to α-la, only β-lactoglobulin (β-lg) formed a heat-induced complex with this protein. This complex was identical in milk ultrafiltrate or in milk and depended on the molar ratio between both proteins; it was not modified by any other milk proteins. The binding of a-la to β-lg changed the ability of the latter protein to bind κ-casein.

Type
Original Articles
Information
Journal of Dairy Research , Volume 43 , Issue 3 , October 1976 , pp. 419 - 432
Copyright
Copyright © Proprietors of Journal of Dairy Research 1976

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References

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