Biochemical characterization and molecular modeling of a unique lipase from Staphylococcus arlettae JPBW-1

Abstract

A three-step purification of a unique lipase with halo-, solvent-, detergent-, and thermo-tolerance from Staphylococcus arlettae JPBW-1 gave raise to a 27-fold purification with a specific activity of 32.5 U/mg. The molecular weight of the purified lipase was estimated to be 45 kDa using SDS–PAGE, and its amino acid sequence was characterized using MALDI-TOF-MS analysis. The sequence obtained from MALDI-TOF-MS showed significant similarity with the capsular polysaccharide biosynthesis protein (CapD) of Staphylococcus aureus through comparative modeling approach using ROBETTA server. Identification of responsible fragments for homodimer formation was performed using comparative modeling and substrate binding domain through C-terminus matching of this new lipase with the CapD of Staphylococcus aureus was executed. Thus, the experimental coupled molecular modeling postulated a structure-activity relationship of lipase from S. arlettae JPBW-1, a potential candidate for detergent, leather, pulp, and paper industries.