Purification and Some Properties of Cell-bound Lipase from Saccharomycopsis lipolytica
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概要
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Two kinds of cell-bound Upases were purified from S. lipolytica with a total recovery of 8%. One was adsorbed and the other not to CM-Sepharose CL-6B at pH 5.0. The method of purification involved chromatography on CM-Sepharose CL-6B, DEAE-Sepharose CL-6B and Sephadex G-100 columns. Sodium dodecylsulfate-polyacrylamide gel electrophoresis of the purified lipases gave a single band. The purified lipases required an activator, such as oleic acid for hydrolysis of triglycerides. The lipases hydrolyzed tricaprylin at the largest initial rate and the optimum pH for hydrolysis of olive oil was about 8.0 under the experimental conditions. They were stable for 20 min below 37°C and in a pH range from 4.5 to 8.0 for 22hr at 5°C. The molecular weight of Lipase I and II was estimated to be 39, 000 and 44, 000, respectively, and both lipases were a monomeric enzyme.
- 社団法人 日本農芸化学会の論文
著者
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Minoda Yasuji
Department Of Agricultural Chemistry Faculty Of Agriculture The University Of Tokyo
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Kato Shigeaki
Department Of Agricultural Chemistry Faculty Of Agriculture Tokyo University Of Agriculture
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Ota Yasuhide
Department Of Applied Biochemistry Faculty Of Applied Biological Science Hiroshima University
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GOMI Komakazu
Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo
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Sugiura Tsutomu
Department O Chemistry Aichi University Of Education
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GOMI Komakazu
Department of Agricultural Chemistry, Faculty of Agriculture
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SUGIURA Tsutomu
Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo
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OTA Yasuhide
Department of Agricultural Chemistry, Faculty of Agriculture
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