Interaction of Bovine α-Lactalbumin and β-Lactoglobulin during Heating
Open Access
- 1 January 1978
- journal article
- research article
- Published by American Dairy Science Association in Journal of Dairy Science
- Vol. 61 (1) , 28-32
- https://doi.org/10.3168/jds.s0022-0302(78)83546-2
Abstract
The degree of thermodenaturation of .alpha.-lactalbumin [cow milk] is greater when heated in the presence of .beta.-lactoglobulin than when heated by itself. This effect increases with temperature and pH (range 6.4-7.2). .alpha.-Lactalbumin interacts with an aggregated form of .beta.-lactoglobulin. .alpha.-Lactalbumin does not affect the amount of undenatured .beta.-lactoglobulin at the end of heating.This publication has 8 references indexed in Scilit:
- Effect of heat on α-lactalbumin and β-lactoglobulin in bovine milkJournal of Dairy Research, 1977
- Serological studies on heat-induced interactions of α-lactalbumin and milk proteinsJournal of Dairy Research, 1976
- A conformational change in bovine β-lactoglobulin at low pHBiochimica et Biophysica Acta (BBA) - Protein Structure, 1975
- β-LactoglobulinsPublished by Elsevier ,1971
- Preparation of α-Lactalbumin from Cow's or Goat's Milk: A Method Improving the YieldJournal of Dairy Science, 1968
- Heat Denaturation of Bovine β-Lactoglobulins and Relevance of Disulfide AggregationJournal of Dairy Science, 1968
- Sulphydryl groups and the N⇄R conformational change in β-lactoglobulinJournal of Molecular Biology, 1966
- Studies on Protein Denaturation. I. Electrophoretic Study Kinetics at Neutrality of Heat Denaturation of β-Lactoglobulin1Journal of the American Chemical Society, 1945