Purification and Characterization of a New Lipase from Fusarium sp. YM-30

Abstract

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 di-acylglycerols, but low toward triacylglycerols. The enzyme had maximum activity at pH 7. 0 to 8. 0 and 37°C, and hydrolyzed digalactosyl diglyceride too.