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.
Research and Development Division, Amano Pharmaceutical Co., Ltd., Aichi, Japan.
T
T
Mase
Y
Y
Matsumiya
T
T
Akiba
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