title: Thermodynamics and inhibition studies of lipozyme TL IM in biodiesel production via enzymatic transesterification.
abstract: In order to characterize enzyme activity and stability corresponding to temperature effects, thermodynamic studies on commercial immobilized lipase have been carried out via enzymatic transesterification. An optimum temperature of 40 degrees C was obtained in the reaction. The decreasing reaction rates beyond the optimum temperature indicated the occurrence of reversible enzyme deactivation. Thermodynamic studies on lipase denaturation exhibited a first-order kinetics pattern, with considerable stability through time shown by the lipase as well. The activation and deactivation energies were 22.15 kJ mol(-1) and 45.18 kJ mol(-1), respectively, implying more energy was required for the irreversible denaturation of the enzyme to occur. At water content of 0.42%, the initial reaction rate and FAME yield displayed optimum values of 3.317 g/L min and 98%, respectively.
authors.affiliation: School of Chemical Engineering, Universiti Sains Malaysia, Nibong Tebal, Pulau Pinang, Malaysia.
authors.forename: Guat Kheng
authors.initials: GK
authors.lastname: Khor
authors.forename: Jia Huey
authors.initials: JH
authors.lastname: Sim
authors.forename: Azlina Harun
authors.initials: AH
authors.lastname: Kamaruddin
authors.forename: Mohamad Hekarl
authors.initials: MH
authors.lastname: Uzir
mesh_terms: D055162:Biocatalysis; D056804:Biofuels; D002849:Chromatography, Gas; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004951:Esterification; D007700:Kinetics; D008049:Lipase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013696:Temperature; D013816:Thermodynamics
chemical_list: D056804:Biofuels; D004800:Enzymes, Immobilized; C093666:Lipozyme; D008049:Lipase