A novel lipase gene, ylip9, of Yarrowia lipolytica MSR80 was cloned and expressed in pEZZ18-HB101 system and was 99 % identical to YLIP9 of Y. lipolytica CLIB122. It was purified using IgG-Sepharose as ZZ fused YLIP9 and had specific activity of 0.8 U/mg. ZZ-YLIP9 was most active at pH 8.0 and 70 A degrees C. It was stable over a wide pH range of 3.0-11.0 and 100 % active at 70 A degrees C up to 2 h and had t (1/2) of 286.42 min at 80 A degrees C. It showed high specificity toward p-nitrophenyldecanoate with k (cat) and catalytic efficiency of 30.17 s(-1) and 16.67 mM(-1) s(-1), respectively. It was non-regioselective, but an S-enantioselective lipase and the percentage conversion were enhanced in presence of hexane. ZZ-YLIP9 was stable in all of the organic solvents used, and its activity was enhanced by solvents having logP value less than 2.