PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR STAPHYLOCOCCUS-WARNERI LIPASE

The extracellular lipase of Staphylococcus warneni was secreted asa pr otein with an apparent molecular mass of 90 kDa. It was then sequentia lly processed in the supernatant to a protein of 45 kDa. Tryptic diges tion of the crude extract resulted in a homogeneous sample containing only the 45-kDa form. Purification was achieved by hydrophobic chromat ography. Purified lipase had an optimum pH of 9.0 and an optimum tempe rature of 25 degrees C. The enzyme was stable within the range pH 5.0- 9.0; it had a broad substrate specificity. The results of inhibition s tudies were consistent with the view that lipases possess a serine res idue at the catalytic site.