Purification and Characterization of a Lipase from the Glycolipid-Producing Yeast Kurtzmanomyces sp. I-11(Biochemistry & Molecular Biology)

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An extracellular lipase produced by the glycolipidproducing yeast Kurtzmanomyces sp. I-11 was purified by ammonium sulfate precipitation and column chromatographies on DEAE-Sephadex A-25, SP-Sephadex C-50, and Sephadex G-100. Based on the analysis of the purified lipase on sodium dodecyl sulfatepolyacrylamide gel electrophoresis, the purified lipase was judged to be homogeneous and its molecular mass was estimated to be approximately 49kDa. The optimum temperature for the activity was 75℃, and the activity was very stable at temperatures below 70℃. The active pH range of this lipase was 1.9-7.2, and the activity was stable at pH below 7.1. The lipase showed a preference for C18 acyl groups by measurements with p-nitrophenyl esters and triglycerides as substrates. The lipase was very stable in the presence of various organic solvents at a concentration of 40%. Although the N-terminal sequence of the Kurtzmanomyces lipase was very similar to that of lipase A from Candida antarctica, the pH profiles of the two lipases were significantly different.
社団法人日本農芸化学会の論文
2002-05-23