Kinetic resolution of ibuprofen catalyzed by Candida rugosa lipase in ionic liquids.
Candida rugosa lipase-catalyzed esterification of ibuprofen with 1-propanol was conducted in seven ionic liquids and the results were compared with those in isooctane. Although the enzyme showed comparable or higher activity in some ionic liquids compared to that in isooctane, only in the case of [BMIM]PF6 was the enantioselectivity (E = 24.1) almost twice that (E = 13.0) of isooctane. In another six ionic liquids the enzyme enantioselectivity was much poorer (E = 1.1-6.4). At the same conversion of 30%, E of [BMIM]PF6 is more than triple that of isooctane. The lipase stability in [BMIM]PF6 was improved by 25% of that in isooctane. It was concluded that [BMIM]PF6 could be applied to substitute the conventional organic solvent (isooctane) in the esterification of ibuprofen.
Hongwei
Yu
Y
Chemical and Process Engineering Centre, National University of Singapore, Singapore. cpeyuhw@nus.edu.sg
Jinchuan
Wu
W
Chi Bun
Ching
C
D002175:Candida / Q000201:enzymology*; D002384:Catalysis; D004795:Enzyme Stability; D007052:Ibuprofen / Q000737:chemistry*; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D013237:Stereoisomerism; D013696:Temperature
D008049:Lipase; D007052:Ibuprofen