title: Kinetic properties of a novel Fusarium solani (phospho)lipase: a monolayer study.
abstract: Using the monomolecular film technique, we studied interfacial properties of Fusarium solani lipase (FSL). This lipolytic enzyme was found to be unique among the fungal lipases possessing not only a lipase activity but also a high phospholipase one.The FSL was able to hydrolyze dicaprin films at various surface pressures. The surface pressure dependency, the stereospecificity, and the regioselectivity of FSL were performed using optically pure stereoisomers of diglyceride (1,2-sn- dicaprin and 2,3-sn-dicaprin) and a prochiral isomer (1,3-sn-dicaprin) spread as monomolecular films at the air-water interface. The FSL prefers adjacent ester groups of the diglyceride isomers (1,2-sn-dicaprin and 2,3-sn-dicaprin) at low and high surface pressures. Furthermore, FSL was found to be markedly stereospecific for the sn-1 position of the 1,2-sn-enantiomer of dicaprin at both low and high surface pressures.Moreover, FSL shows high activities on phospholipids monolayers. However, this enzyme displays high preference to zwitterionic phospholipids compared to the negatively charged ones.
authors.affiliation: Laboratoire de Biochimie et de Génie Enzymatique des Lipases, ENIS, Université de Sfax, Route de Soukra, 3038 Sfax, Tunisia.
authors.forename: Raida
authors.initials: R
authors.lastname: Jallouli
authors.forename: Ahmed
authors.initials: A
authors.lastname: Fendri
authors.forename: Tahar
authors.initials: T
authors.lastname: Mechichi
authors.forename: Youssef Talèl
authors.initials: YT
authors.lastname: Gargouri
authors.forename: Sofiane
authors.initials: S
authors.lastname: Bezzine
mesh_terms: D005670:Fusarium / Q000201:enzymology*; D007700:Kinetics; D010740:Phospholipases / Q000737:chemistry / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism; D011312:Pressure
chemical_list: D010743:Phospholipids; D010740:Phospholipases