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Solvent effects in lipase-catalysed transesterification reactions.
L T Kanerva1, J Vihanto, M H Halme
1Department of Chemistry, University of Turku, Finland.
Acta Chemica Scandinavica (Copenhagen, Denmark : 1989)
|November 1, 1990
Summary
This study shows that solvent hydrophobicity minimally impacts lipase-catalyzed transesterification rates. High optical purity of ester products was achieved regardless of the organic solvent used.
Area of Science:
- Biocatalysis
- Organic Chemistry
- Enzyme kinetics
Background:
- Lipases are versatile enzymes for synthesis.
- Transesterification is a key reaction catalyzed by lipases.
- Solvent effects on enzyme activity are crucial for optimizing reactions.
Purpose of the Study:
- To investigate the effect of solvent hydrophobicity on porcine pancreatic lipase-catalyzed transesterification.
- To evaluate the enantioselectivity of the lipase in various organic solvents.
- To compare the activity of porcine pancreatic lipase with Candida cylindracea lipase.
Main Methods:
- Enzymatic transesterification using porcine pancreatic lipase.
- Reaction of 2,2,2-trifluoroethyl butyrate with racemic 2-octanol and 1-phenylethanol.
- Screening of organic solvents with varying hydrophobicity (log P).
- Analysis of reaction rates and enantiomeric excess (ee) of products.
Main Results:
- Solvent hydrophobicity showed a minor effect on the reaction rate of porcine pancreatic lipase.
- High enantiomeric purity (ee > 90%) of (R)-2-octyl and (R)-1-phenylethyl butyrates was achieved across different solvents.
- Candida cylindracea lipase demonstrated activity only in highly hydrophobic solvents.
Conclusions:
- Porcine pancreatic lipase is effective for kinetic resolution of racemic alcohols via transesterification.
- The choice of solvent has a limited impact on the efficiency and enantioselectivity of this lipase.
- Enzyme selection is critical, as different lipases exhibit distinct solvent preferences.