Peculiar properties of lipase fromCandida parapsilosis (Ashford) langeron and talice

A new Candida parapsilosis lipase was isolated and studied. This enzyme was purified by hydrophobic chromatography on a phenyl‐sepharose CL4B column followed by gel permeation on a Sephacryl S300 HR column. It was a 160 kg·mol −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.