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Enantiomeric partitioning using fluorous biphase methodology for lipase-mediated (trans)esterifications
1School of Chemistry, Centre for Biomolecular Sciences, University of St Andrews, North Haugh, St Andrews, Fife, UK KY16 9ST.
Chemical Communications (Cambridge, England)
|August 29, 2002
Summary
Enzyme-catalyzed transesterification reactions in specialized solvents allow for direct separation of enantiomers, achieving high enantiomeric excess (ee) up to 95%. This method simplifies chiral compound purification using liquid-liquid separation.
Area of Science:
- Biocatalysis
- Organic Chemistry
- Separation Science
Background:
- Lipase-catalyzed reactions are crucial for synthesizing chiral compounds.
- Achieving high enantiomeric purity often requires complex separation techniques.
- Homogenous solvent systems can facilitate biocatalytic processes.
Purpose of the Study:
- To investigate lipase-catalyzed transesterification in mixed solvents.
- To develop a method for direct enantiomeric partitioning of reaction products.
- To achieve high enantiomeric excess (ee) through simple separation.
Main Methods:
- Utilizing lipase as a biocatalyst for transesterification.
- Employing a homogenous mixture of perfluorocarbon and hydrocarbon solvents.
- Implementing liquid-liquid separation for product partitioning.
Main Results:
- Successful lipase-catalyzed transesterification was achieved in the mixed solvent system.
- Direct enantiomeric partitioning of products was enabled by liquid-liquid separation.
- Enantiomeric excess (ee) of up to 95% was obtained for the products.
Conclusions:
- Lipase-catalyzed transesterification in perfluorocarbon-hydrocarbon solvents is an effective strategy.
- Direct enantiomeric partitioning via liquid-liquid separation simplifies chiral product purification.
- This approach offers a high-yield, high-purity method for producing enantiomerically enriched compounds.