Thermodynamics and inhibition studies of lipozyme TL IM in biodiesel production via enzymatic transesterification

• Published in: Bioresource technology Vol. 101; no. 16; pp. 6558 - 6561
• Main Authors: Khor, Guat Kheng, Sim, Jia Huey, Kamaruddin, Azlina Harun, Uzir, Mohamad Hekarl
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 01.08.2010; [New York, NY]: Elsevier Ltd; Elsevier
• Subjects: Activation energy; Biocatalysis; Biodiesel; Biofuel production; Biofuels; Biological and medical sciences; Biotechnology; Chromatography, Gas; Deactivation; Denaturation; Energy; Enzymes, Immobilized - metabolism; Esterification; Fundamental and applied biological sciences. Psychology; Industrial applications and implications. Economical aspects; Kinetics; Lipase; Lipase - antagonists & inhibitors; Lipase - metabolism; Lipozyme TL IM; Optimization; Stability; Temperature; Thermodynamics; Transesterification; Water content; Thermodynamics; Temperature; Lipozyme TL IM; Biodiesel; Water content; Enzyme; Inhibition; Transesterification
• ISSN: 0960-8524; 1873-2976
• DOI: 10.1016/j.biortech.2010.03.047

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 °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.