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Abstract The kinetics of Candida rugosa lipase catalyzed esterification of racemic ibuprofen with n-butanol inisooctane was studied.The kinetic study was carried out with the addition of 0.1% and 2% (by volume) of waterfor enzyme activation respectively when celite was added into isooctane for enzyme dispersion.The specific initialrate for S-ibuprofen can be fitted with the Ping Pong Bi Bi mechanism with dead-end competitive inhibition by thealcohol.The time courses of the enantioselective esterification of the two ibuprofen enantiomers with different initialsubstrate concentrations and water contents were simulated with a model in which both effects of enzyme inactivationby long term reaction and reversed hydrolytic reaction under high water content were taken into consideration.
Abstract The kinetics of Candida rugosa lipase catalyzed esterification of racemic ibuprofen with n-butanol in isooctane was studied. Kinetic study was carried out with the addition of 0.1% and 2% (by volume) of water for enzyme activation not when celite was added into isooctane for enzyme dispersion. The specific initialrate 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 initialsubstrate concentrations and water contents were simulated with a model in which both both effects of enzyme inactivationby long term reaction and high water content were taken into consideration.