title: [Isolation and characteristics of Penicillium roqueforti lipases].
abstract: Lipase were isolated from Penicillium roqueforti 141, purified and their properties were studied. Proteins were precipitated with (NH4)2SO4 from the cultural broth of this organism, and then subjected to gel filtration through Sephadex G-100 and chromatography on DEAE-cellulose; the procedure yielded a purified preparation consisting of three lipolytically active proteins. Disc electrophoresis in polyacrylamide gel confirmed the homogeneity of the lipases. The molecular weights of the enzymes were 7930, 9100 and 11 420 respectively, according to the data of gel filtration through Sephadex G-150. The lipases differed in their substrate specificity. Lipase III was most active in hydrolysis of plant oils containing mainly unsaturated fatty acids. Lipase II most effectively hydrolyzed synthetic triglycerides containing saturated fatty acids, in particular, tricaproin, tricaprilin and trimyristin. Tributyrin was more actively hydrolyzed with lipase I as compared to lipases II and III.
mesh_terms: D004789:Enzyme Activation; D008049:Lipase / Q000032:analysis / Q000302:isolation & purification*; D008722:Methods; D008970:Molecular Weight; D010407:Penicillium / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D008049:Lipase
vernacular_title: Vydelenie i nekotorye svoĭstva lipaz Penicillilum roqueforti.