By gel chromatography and polyacrylamide gel disc-electrophoresis the component composition of the culture liquid separated from the mycelium was investigated. After elution from Sephadex G-75 column lipase activity was concentrated in one peak. Out of 13 electrophoretic mobile protein components only one split trioleate. The paper describes a method to isolate lipase from the native solution of the produced which involves enzyme precipitation at 40% saturation of the native solution with ammonium sulphate, dialysis of the resultant concentrate and selective sorption of pigment and protein admixtures on the cellulose anion exchanger. The method maker it possible to obtain a highly purified lipolytic enzyme with a specific activity of up to 15 000 lu/mg protein and to provide its 35--40% yield.