Abstract
The heat-induced interaction of β-lactoglobulin (β-Lg) and κ-casein has received much study, but comparatively little work has been done on heat-induced interactions among the whey proteins. It has been suggested that an interaction may occur between β-Lg and α-lactalbumin (α-La) when these proteins mixed in solution are heated (3, 4, 8). Yamauchi (8), after heating whey proteins for 10 min at 70 C in. dilute sodium chloride solution, found a new electrophoretic peak between α-La and β-Lg. Hostettler and Stein (3) reported that the protein in the sediment from stored evaporated milk contained an α-La-β-Lg complex whose electrophoretic mobility was intermediate between those of the proteins singly. This study presents chromatographic evidence for the heat-induced interaction between α-La and β-Lg.
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