Journal of Chemical Technology and Biotechnology, Vol.75, No.8, 715-721, 2000
Lipase-catalysed esterification of oleic acid and ethanol in a continuous packed bed reactor, using supercritical CO2 as solvent: approximation of system kinetics
This work investigated the immobilised Lipase kinetics of esterification of oleic acid and ethanol. The reaction was conducted under supercritical conditions (13 x 10(6)Pa and 40 degrees C) using carbon dioxide as solvent in a continuous packed bed (plug flow) reactor. Biocatalyst Lypozyme(TM) IM60, which is lipase from Rhizomucor miehei (EC.3.1.1.3), immobilised on Duolite (anionic exchange resin) was used as biocatalyst. Kinetically, with regard to oleic acid, the reaction was successfully modelled by the Michaelis-Menten mechanism. The reaction rate constants K-m and V-max were evaluated. Furthermore, it was found to undergo competitive inhibition by ethanol, and the inhibition constant K-i was evaluated.
Keywords:immobilised lipase;kinetics;esterification;supercritical CO2;Michaelis-Menten;substrate inhibition;biocatalysis