Journal
FOOD HYDROCOLLOIDS
Volume 16, Issue 4, Pages 303-311Publisher
ELSEVIER SCI LTD
DOI: 10.1016/S0268-005X(01)00103-5
Keywords
emulsions; protein adsorption; heating effects; caseins; whey proteins
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The heat-induced exchange of caseins and serum proteins on the interfaces of oil-in-water emulsion droplets has been studied. At temperatures above 40degreesC, the proteins from whey protein isolate were capable of displacing adsorbed caseins. As the whey proteins beta-lactoglobulin and alpha-lactalbumin adsorbed, alpha(s1)- and beta-caseins were desorbed, principally the former. The alpha(s2)- and kappa-caseins were not displaced. The rate of the displacement or exchange reaction was temperature-dependent, being almost undetectable at room temperature, but complete within 2 min at 80degreesC. The extent to which the caseins were displaced by whey proteins was also temperature dependent. The displacement reaction was neither affected by ionic strength, nor were any of the reactions apparently dependent on sulphydryl exchange reactions. On the other hand, the extents of displacement of the major caseins by the whey proteins were pH-dependent to a limited extent. It is evident that the behavior is not simply governed by equilibrium processes between adsorbed and non-adsorbed proteins, and this is discussed. (C) 2002 Elsevier Science Ltd. All rights reserved.
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