Purification of the intracellular triacylglycerol lipase ofOospora lactis

A method for the isolation of homogeneous triacylglycerol hydrolase from the mycelium of the fungusOospora lactis is described. The homogeneity of the enzyme has been shown by gel filtration through Sephadex G-100, by ultracentrifugation, and by disc electrophoresis in polyacrylamide gel. Some properties of the enzyme have been studied: molecular weight, 43,000; optimum action temperature, 35–37°C; pH optimum, 7.5.