Influence of other whey proteins on the heat-induced aggregation of α-lactalbumin
1993
Calvo, Marta M. | Leaver, J. | Banks, J. M. | North Atlantic Treaty Organization | Scottish Government's Rural and Environment Science and Analytical Services | Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
The thermally induced aggregation of α-lactalbumin in solution and in the presence of serum protein-free casein micelles has been studied using gel permeation chromatography. No aggregation of α-lactalbumin was detected after heating at 90°C for 24 min. However, addition of β-lactoglobulin or serum albumin to the serum protein-free casein micelles + α-lactalbumin system caused aggregation of the α-lactalbumin, the rate and extent of this aggregation being dependent upon the concentration of free sulphydryl groups present in the other whey protein. It is therefore the sulphydryl group which is important and which appears to function by inducing cleavage of intramolecular disulphide bonds in the α-lactalbumin. This leads to the formation of intermolecular disulphide bridges and hence to aggregation of the α-lactalbumin.
显示更多 [+] 显示较少 [-]One of the authors (M. M. C.) thanks NATO for financial support during the course of this work. The research was also funded by The Scottish Office Agriculture and Fisheries Department.
显示更多 [+] 显示较少 [-]Peer reviewed
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