Chromatographic Evidence for Heat-Induced Interaction of α-Lactalbumin and β-Lactoglobulin

The heat-induced interaction of p-lactoglobulin (P-Lg) and K-casein has received much study, but comparatively little work has been done on heat-induced interactions among the whey proteins. I t has been suggested that an interaction may occur between P-Lg and a-lactalbuniin (a-La) when these proteins mixed in solution are heated Yanlauchi (S), after heating whey proteins f o r 10 rnin a t 70 C in dilute sodiu~n chloride solution, found a new electrophoretic peak between a-La and P-Lg. Hostettler and Steiu (3) reported that the proteiu in the sediment from stored evaporated milk coutained a n a-La-&Lg complex whose electrophoretic mobility was intermediate between those of the proteins singly. This study presents chromatographic evidence f o r the heat-induced interaction between a-La and 8-Lg .