Purification and characterization of a new lipase from Fusarium sp. YM-30.
The extracellular lipase from Fusarium sp. YM-30 was purified by a procedure involving ultrafiltration, ammonium sulfate precipitation, and DEAE-Toyopearl 650M, CM-Toyopearl 650M, and Butyl-Toyopearl 650M column chromatographies. The purified lipase was homogeneous with 12kDa of molecular mass by SDS-PAGE, and had high specificities for mono- and diacylglycerols, but low toward triacylglycerols. The enzyme had maximum activity at pH 7.0 to 8.0 and 37 degrees C, and hydrolyzed digalactosyl diglyceride too.
Mase
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Research and Development Division, Amano Pharmaceutical Co., Ltd., Aichi, Japan.
Matsumiya
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Y
Akiba
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D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D005670:Fusarium / Q000201:enzymology* / Q000378:metabolism; D008049:Lipase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification*; D008670:Metals / Q000494:pharmacology; D013379:Substrate Specificity
D008670:Metals; D008049:Lipase