The kinetics of Candida rugosa lipase catalyzed esterification of racemic ibuprofen with n-butanol in isooctane was studied. The kinetic study was carried out with the addition of 0.1% and 2% (by volume) of water for ...The kinetics of Candida rugosa lipase catalyzed esterification of racemic ibuprofen with n-butanol in isooctane was studied. The kinetic study was carried out with the addition of 0.1% and 2% (by volume) of water for enzyme activation respectively when celite was added into isooctane for enzyme dispersion. The specific initial rate for S-ibuprofen can be fitted with the Ping Pong Bi Bi mechanism with dead-end competitive inhibition by the alcohol. The time courses of the enantioselective esterification of the two ibuprofen enantiomers with different initial substrate concentrations and water contents were simulated with a model in which both effects of enzyme inactivation by long term reaction and reversed hydrolytic reaction under high water content were taken into consideration.展开更多
文摘The kinetics of Candida rugosa lipase catalyzed esterification of racemic ibuprofen with n-butanol in isooctane was studied. The kinetic study was carried out with the addition of 0.1% and 2% (by volume) of water for enzyme activation respectively when celite was added into isooctane for enzyme dispersion. The specific initial rate for S-ibuprofen can be fitted with the Ping Pong Bi Bi mechanism with dead-end competitive inhibition by the alcohol. The time courses of the enantioselective esterification of the two ibuprofen enantiomers with different initial substrate concentrations and water contents were simulated with a model in which both effects of enzyme inactivation by long term reaction and reversed hydrolytic reaction under high water content were taken into consideration.
