| Literature DB >> 20211549 |
Abstract
The heat-induced changes in the surface protein compositions and concentrations of whey protein isolate (WPI)-stabilized emulsions were examined. With increasing heating temperature, the amount of adsorbed beta-lactoglobulin (beta-lg) increased whereas the amount of adsorbed alpha-lactalbumin (alpha-la) decreased. In emulsions formed with 0.5 wt% WPI, the adsorbed alpha-la almost disappeared from the interface of the emulsion droplets after heating at 121 degrees C. With heat treatment at 90 degrees C, adsorbed beta-lg increased but adsorbed alpha-la decreased in the first 5 min, and then changed slightly with increasing heating time. This change in the proportions of beta-lg and alpha-la at the interface may have arisen from the displacement of alpha-la from the interface by beta-lg in the aqueous phase. The addition of NaCl resulted in an increase in the total surface protein concentration during heat treatment, but the competition between beta-lg and alpha-la at high temperatures was eliminated. The emulsions lost stability because bridging flocculation of the emulsion droplets occurred during heat treatment in the presence of NaCl (>50 mM). Copyright 2010 Elsevier B.V. All rights reserved.Entities:
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Year: 2010 PMID: 20211549 DOI: 10.1016/j.colsurfb.2010.02.001
Source DB: PubMed Journal: Colloids Surf B Biointerfaces ISSN: 0927-7765 Impact factor: 5.268