Thermodynamics and inhibition studies of lipozyme TL IM in biodiesel production via enzymatic transesterification.
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.
Khor
Guat Kheng
GK
School of Chemical Engineering, Universiti Sains Malaysia, Nibong Tebal, Pulau Pinang, Malaysia.
Sim
Jia Huey
JH
Kamaruddin
Azlina Harun
AH
Uzir
Mohamad Hekarl
MH
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
D056804:Biofuels; D004800:Enzymes, Immobilized; C093666:Lipozyme; D008049:Lipase