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 chromatographies. The purified lipase was homogeneous with 25 kDa of molecular mass by SDS–polyacrylamide gel electrophoresis, and had high specificities toward short-chain fatty acid esters.
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