Purification and Some Properties of Cell-bound Lipase from Saccharomycopsis lipolytica
1982 Volume 46 Issue 12 Pages 2885-2893
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1982 Volume 46 Issue 12 Pages 2885-2893
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.
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