Purification and Characterization of Penicillium roqueforti IAM 7268 Lipase

Abstract

An extracellular lipase from Penicillium roqueforti IAM 7268 was purified by a procedure involving ethanol precipitation, ammonium sulfate precipitation, and DEAE-Toyopearl 650M, Phenyl-Toyopearl 650M, and Toyopearl HW-60 column chromatog-raphies. The purified lipase was homogeneous with 25kDa of molecular mass by SDS-polyacrylamide gel electrophoresis, and had high specificities toward short-chain fatty acid esters.