Lobyreva L B, Marchenkova A I
Mikrobiologiia. 1980 Nov-Dec;49(6):924-30.
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.
从罗克福青霉141中分离出脂肪酶，进行纯化并研究其性质。用硫酸铵从该微生物的培养液中沉淀蛋白质，然后通过Sephadex G - 100进行凝胶过滤并在DEAE - 纤维素上进行色谱分析；该程序得到了一种由三种具有脂解活性的蛋白质组成的纯化制剂。聚丙烯酰胺凝胶中的圆盘电泳证实了脂肪酶的均一性。根据通过Sephadex G - 150凝胶过滤的数据，这些酶的分子量分别为7930、9100和11420。这些脂肪酶的底物特异性不同。脂肪酶III在水解主要含有不饱和脂肪酸的植物油方面活性最高。脂肪酶II最有效地水解含有饱和脂肪酸的合成甘油三酯，特别是三己酸甘油酯、三辛酸甘油酯和十四酸甘油酯。与脂肪酶II和III相比，脂肪酶I对三丁酸甘油酯的水解更活跃。
