PECULIAR PROPERTIES OF LIPASE FROM CANDIDA-PARAPSILOSIS (ASHFORD) LANGERON AND TALICE

A new Candida parapsilosis lipase was isolated and studied. This enzym e was purified by hydrophobic chromatography on a phenyl-sepharose CL4 B column followed by gel permeation on a Sephacryl S300 HR column. It was a 160 kg.mol-1 molecular-weight oligomeric enzyme. Optimal activit y was obtained at 45-degrees-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 lip ase showed a high specificity for long-chain fatty acids and particula rly for polyunsaturated fatty acids. This enzyme was able to catalyze the synthesis of various oleoylesters in aqueous medium.