Commercial immobilized lipase B from Candida antarctica (CALB) was successfully applied to catalyzing the transesterification of (R, S)-1-phenylethanol in supercritical carbon dioxide (SC CO2) and in supercritical carbon dioxide/ionic liquid biphasic system. The influence of CALB concentration, temperature and pressure on the performance of CALB in transesterification reactions in SC CO2 were studied. For transesterification, performed in SC CO2/ionic liquid biphasic system, influence of 1-butyl-3-methylimidazolium tetrafluoroborate concentration on reaction performance was studied.
COBISS.SI-ID: 13823766
The kinetic resolution of racemates represents a major route to manufacture optically pure compounds. The enzymatic kinetic resolution of (R,S)-1-phenylethanol with Candida antarctica lipase B (CALB) using vinyl acetate as the acyl donor in the acylation reaction was chosen as model reaction. Optimization of the reaction parameters with respect to the final product concentration was performed. Enantioselectivity of CALB was assayed in several ionic liquids. After 3 h of bioconversion, the highest possible conversion (50%) was reached with enantiomeric excess for substrate higher than 99%.
COBISS.SI-ID: 12966422