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A new Candida parapsilosis lipase was isolated and studied. This enzyme was purified by hydrophobic chromatography on a phenyl-sepharose CIAB column followed by gel permeation on a Sephacryl $300 HR column. It was a 160 kg'mo1-1 molecular-weight oligomeric enzyme. Optimal activity was obtained at 45°C and pH 6.5. The lipase activity toward various acylglycerols and esters was studied. The hydrolysis rate was greater for secondary acylesters than for primary acylesters. This lipase showed a high specificity for long-chain fatty acids and particularly for polyunsaturated fatty acids. This enzyme was able to catalyze the synthesis of various oleoylesters in aqueous medium.

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