Studies on Bile-sensitive Lipase. V. Purification and Properties of Lipase from Mucor javanicus
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It had been found that in one of lipase [EC 3. 1. 1. 3] from Mucor javanicus the hydrolysis of fats was accelerated by bile salts. The lipase was purified about 20-fold from the original powder (about 100-fold from the culture broth) by ammonium sulfate precipitation, chromatography on Sephadex G-75,CM-cellulose, and Sephadex G-200. Recovery of the activity was about 18%. The purified enzyme was homogeneous on electrophoresis. Optimum pH for hydrolysis of olive oil was 7.0 by the assay method using a PVA system and 7.5 by that using a shaken system. Optimum temperature was 40°. The enzyme was stable below 30°. It was strongly inhibited by Ag^+, Hg^<2+>, and N-bromosuccinimide (NBS). The apparent I_<50> value of NBS was 1.4×10^<-4>M, that of both iodine and sodium lauryl sulfate were 2.4×10^<-3>M. The lipase hydrolyzed tricaprylin most efficiently, and next to it tricaprin and trilaurin. The Michaelis constant (Km) for triglycerides agreed closely with the substrate specificity.
- 公益社団法人日本薬学会の論文
- 1969-05-25
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