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

Guat Kheng Khor, Jia Huey Sim, Azlina Harun Kamaruddin, Mohamad Hekarl Uzir

School of Chemical Engineering, Universiti Sains Malaysia, Nibong Tebal, Pulau Pinang, Malaysia.

Bioresource technology 2010 Aug

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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. Copyright 2010 Elsevier Ltd. All rights reserved.

Citation

Guat Kheng Khor, Jia Huey Sim, Azlina Harun Kamaruddin, Mohamad Hekarl Uzir. Thermodynamics and inhibition studies of lipozyme TL IM in biodiesel production via enzymatic transesterification. Bioresource technology. 2010 Aug;101(16):6558-61