Abstract
A simplified kinetic model for the enzyme-catalyzed irreversible transesterification in organic solvents was proposed by considering the hydrolysis and esterification side reactions. The analysis was extended to the kinetic resolution of activated racemic esters containing a chiral center in the acid moiety, and was confirmed from the lipase-catalyzed enantioselective transesterification between (R,S)-suprofen 2,2,2-trifluoroethyl ester and 2-N-morpholinoethanol (or di(ethylene glycol)) in cyclohexane. Theoretical analysis indicates that the time-course yield and/or the enantiomeric excess for the desired (S)-ester product may be improved if the employed enzyme has a higher activity and/or enantioselectivity for the hydrolysis and esterification than the transesterification. (C) 2000 Elsevier Science Ltd. All rights reserved.
Original language | English |
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Pages (from-to) | 4571-4582 |
Number of pages | 12 |
Journal | Chemical Engineering Science |
Volume | 55 |
Issue number | 20 |
DOIs | |
State | Published - 10 2000 |
Externally published | Yes |
Keywords
- Esterification
- Hydrolysis
- Irreversible transesterification
- Kinetic resolution
- Lipase
- Suprofen esters