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

Research paper by Guat Kheng GK Khor, Jia Huey JH Sim, Azlina Harun AH Kamaruddin, Mohamad Hekarl MH Uzir

Indexed on: 07 Apr '10Published on: 07 Apr '10Published in: Bioresource Technology


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.