title: Kinetic and thermodynamic characterization of lipase produced by Cellulomonas flavigena UNP3.
abstract: Lipase of Cellulomonas flavigena UNP3 was purified by two-step purification process comprising ammonium sulfate precipitation followed by gel permeation chromatography (GPC). The recovery of lipase after GPC was found to be 1.70% with 20.98-fold increase in specific activity. The molecular weight of lipase protein was found to be 45.2 kDa by SDS-PAGE. Activation energy for p-nitrophenol palmitate (pNPP) hydrolysis was 26.45 kJ mol(-1) , while temperature quotient (Q10 ) was found to be 1.64. The enzyme was found to be stable over wide pH range and thermally stable at 30-40 °C up to 60 min of incubation while exhibited maximum activity at 30 °C with pH 7.0. Vmax , Km , and Kcat for pNPP were found to be 666.71 U ml(-1) , 1.33 mM (pNPP) and 433 min(-1) , respectively. Activation energy for irreversible inactivation Ea(d) of lipase was 64.32 kJ mol(-1) . Thermodynamic parameters of irreversible inactivation of lipase and pNPP hydrolysis were also determined.
authors.affiliation: B R D School of Biosciences, Sardar Patel University, Sardar Patel Maidan, Vadtal Road, Vallabh Vidyanagar, Gujarat, India.
authors.forename: Vimal
authors.initials: V
authors.lastname: Prajapati
authors.forename: Honey
authors.initials: H
authors.lastname: Patel
authors.forename: Ujjval
authors.initials: U
authors.lastname: Trivedi
authors.forename: Kamlesh
authors.initials: K
authors.lastname: Patel
mesh_terms: D040143:Cellulomonas / Q000201:enzymology*; D011232:Chemical Precipitation; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008049:Lipase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D013696:Temperature; D013816:Thermodynamics
chemical_list: D008049:Lipase
keywords: Cellulomonas flavigena UNP3; Kinetics; Lipase; Thermodynamics