Kinetic properties of a novel Fusarium solani (phospho)lipase: a monolayer study.

ABSTRACT Using the monomolecular film technique, we studied interfacial properties ofFusarium solani lipase (FSL). This lipolytic enzyme was found to be unique among the fungallipases possessing not only a lipase activity but also a high phospholipase one.The FSL was ableto hydrolyze dicaprin films at various surface pressures. The surface pressure dependency, thestereospecificity,andtheregioselectivityofFSLwereperformedusingopticallypurestereoisomersofdiglyceride(1,2-sn-dicaprinand2,3-sn-dicaprin)andaprochiralisomer(1,3- sn-dicaprin)spreadasmonomolecular films at the air–water interface. The FSL prefers adjacent ester groups of thediglycerideisomers(1,2-sn-dicaprinand2,3-sn-dicaprin)atlowandhighsurfacepressures.Further-more, FSL was found to be markedly stereospecific for the sn-1 position of the 1,2-sn-enantiomer ofdicaprin at both low and high surface pressures.Moreover, FSL shows high activities on phospholi-pids monolayers. However, this enzyme displays h igh preference to zwitterionic phospholipidscomparedtothenegativelychargedones. Chirality,00:000-000,2012. ©2012WileyPeriodicals,Inc.KEY WORDS: (phospho)lipase; phospholipids monolayer; regioselectivity; stereospecifity