Solvent Effects in Lipase-Catalysed Transesterification Reactions.
- 1 January 1990
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 44 (10) , 1032-1035
- https://doi.org/10.3891/acta.chem.scand.44-1032
Abstract
Porcine pancreatic lipase-catalysed transesterifications of 2,2,2-trifluoroethyl butyrate with racemic 2-octanol and 1-phenylethanol have been studied in different organic solvents. Solvent hydrophobicity (log P -1.1 to 3.3) has only a minor effect on the reaction rate. Independently of the solvent used as the reaction medium, both (R)-2-octyl and (R)-1-phenylethyl butyrates were obtained in high optical purity (ee >90%). Candida cylindracea lipase is active only in the most hydrophobic solvents studied.This publication has 1 reference indexed in Scilit:
- Enzyme-catalyzed processes in organic solvents.Proceedings of the National Academy of Sciences, 1985