Enhanced activity and enantioselectivity of Candida rugosa lipase immobilized on macroporous adsorptive resins for ibuprofen resolution.
The lipase from Candida rugosa was immobilized on three commercially available macroporous adsorptive resins for kinetic resolution of ibuprofen. One resin, CRB02, increased the enzyme activity by 50% to 0.027 g g(-1) min(-1). The deactivation constant (0.19 h(-1)) of the immobilized enzyme was half of that of the native enzyme and the enantioselectivity (E = 29.2) of the immobilized lipase was 2.2 times as much as that of the native lipase for the kinetic resolution of ibuprofen with 1-propanol in isooctane at 30 degrees C.
Yu
Hongwei
H
Chemical and Process Engineering Centre, National University of Singapore, 4 Engineering Drive 4, Singapore. cpeyuhw@nus.edu.sg
Wu
Jinchuan
J
Ching
Chi Bun
CB
D000327:Adsorption; D002175:Candida / Q000737:chemistry / Q000201:enzymology*; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D007052:Ibuprofen / Q000737:chemistry* / Q000302:isolation & purification; D007700:Kinetics; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism*; D012117:Resins, Synthetic / Q000737:chemistry*; D013237:Stereoisomerism; D015854:Up-Regulation
D004800:Enzymes, Immobilized; D012117:Resins, Synthetic; D008049:Lipase; D007052:Ibuprofen