Purification and characterization of extracellular Staphylococcus warneri lipase

Abstract
The extracellular lipase of Staphylococcus warneri was secreted as a protein with an apparent molecular mass of 90 kDa. It was then sequentially processed in the supernatant to a protein of 45 kDa. Tryptic digestion of the crude extract resulted in a homogeneous sample containing only the 45-kDa form. Purification was achieved by hydrophobic chromatography. Purified lipase had an optimum pH of 9.0 and an optimum temperature of 25°C. The enzyme was stable within the range pH 5.0–9.0; it had a broad substrate specificity. The results of inhibition studies were consistent with the view that lipases possess a serine residue at the catalytic site.