Dialyzed skimmilk was fractionated by DEAE cellulose column chromatography. The major chromatographic components were identified by starch gel eleetrophoresis with urea. Lipase activity, measured with milk fat as substrate at pH 9.0, was demonstrated in several fractions where K-casein was present. Other casein components appeared free of lipase activity. Lipase specific activity was correlated with the amount of sialic acid in the lipase-active casein fractions. No lipase activity was detected in whey protein fractions. Results indicate that the major milk lipase is a part of the K-casein complex or K-casein itself.
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Yaguchi et al. (1964) studied this question.