Purification and Some Properties of a Thermostable Lipase from Humicola lanuginosa No.3(Microbiology & Fermentation Industry)
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概要
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A thermostable lipase from Humicola lanuginosa No. 3 was purified by means of acetone precipitation and successive chromatographies on Sephadex G-75, DEAE Sepharose CL-6B and hydroxyapatite columns. The enzyme was purified about 150-fold with a yield of 15.0% and a specific activity of about 3000 U/mg protein. The purified enzyme showed a single protein band on polyacrylamide gel electrophoresis. Its molecular weight was estimated to be 39,000 on both sodium dodecyl sulfate polyacrylamide gel electrophoresis and gel filtration on Sephadex G-100, suggesting that the enzyme was a monomer. Its isoelectric point was pH 6.6. The optimum pH and temperature were 7.0 and 45℃, respectively. The enzyme was stable over a pH range of 5 to 9 (45℃, 24hr), and its activity was maintained at 60℃ for about 20hr. The activity was inhibited by Co^<2+>, Cu^<2+>, Ni^<2+>, Hg^<2+> and Sn^<2+>, and slightly affected by Zn^<2+>, Mg^<2+>, EDTA and sodium dodecyl sulfate. The Km value for trilaurin (45℃) was 14.2mg/ml. The enzyme was specific for substrates containing a C12 fatty acid component. Analysis of hydrolyzates of triolein amd olive oil after the lipase reaction revealed that Humicola lanuginosa No. 3 produced a 1,3 positional specific lipolytic enzyme.
- 社団法人日本農芸化学会の論文
- 1987-01-23
著者
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Nagai Shiro
Department Of Fermentation Technology Faculty Of Engineering Hiroshima University
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Hayashi Mitsunori
Department Of Fermentation Technology Faculty Of Engineering Hiroshima University
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IBRAHIM Che
Department of Fermentation Technology, Faculty of Engineering, Hiroshima University
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Ibrahim Che
Department Of Fermentation Technology Faculty Of Engineering Hiroshima University
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