Lipase-catalyzed enantioselective esterification of glycidol in supercritical carbon dioxide

摘要: Abstract The enzymatic resolution of racemic glycidol in supercritical CO2 is described. route chosen was the esterification with butyric acid catalyzed by either free or immobilized porcine pancreatic lipase. solubility glycidol, least soluble reactant, measured at 35°C and pressures range 70–180 bar for concentrations up to 500 mM. pressure selected subsequent experiments 140 bar. partitioning water between enzyme preparations quantified various amounts added water. experimental sorption isotherms obtained were used derive content assayed kinetic studies. For enzyme, maximum reaction rates an 10 ± 2% w/w, same as organic solvents, although corresponding initial rate 0.0045 0.0003 m h−1 g−1 much lower than these solvents. A series supports covering a wide hydrophilicities screened activity, best results being more hydrophilic ones, Sephadex G-25 Bio-gel P6. Enzyme on performed better leading optimized 0.0110 0.0007 purities 83 (S)-glycidyl butyrate, 25–30% conversion 20–25% hydration preparations. selectivity observed highest value As those enantioselectivity does not depend hydration.