抄録
The lipase-catalyzed acetylation of 2-alkanol with vinyl acetate was studied using Burkholderia cepacia lipase (BCL), three alcohol and three organic solvents in a packed-bet reactor with a recycling system (flow method). The optical resolution data were found in agreement with those of the batch method in which BCL was suspended in the substrate solution. Repeated reaction results clearly indicated BCL in the packed-bed to be quite stable and to be usable for at least 50 reaction runs or to remain effective for as long as two months in the water-insoluble solvents such as hexane and 1,2-dichloroethane. In the reaction using a water-soluble solvent such as acetonitrile, the catalytic power of BCL showed only a 1% decrease of conversion per run or solvent recycling possibly owing to compression of BCL in the bed although enantioselectivity was independent of the number of reaction repetitions. The present method showed thus be applicable to kinetic resolution by enzyme-catalyzed acylation in hydrophobic organic solvents with no waste of enzyme.
