Enhanced activity and enantioselectivity of Candida rugosa lipase immobilized on macroporous adsorptive resins for ibuprofen resolution

Biotechnol Lett. 2004 Apr;26(8):629-33. doi: 10.1023/b:bile.0000023020.12576.1e.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Candida / chemistry
  • Candida / enzymology*
  • Enzymes, Immobilized / chemistry
  • Enzymes, Immobilized / metabolism*
  • Ibuprofen / chemistry*
  • Ibuprofen / isolation & purification
  • Kinetics
  • Lipase / chemistry*
  • Lipase / metabolism*
  • Resins, Synthetic / chemistry*
  • Stereoisomerism
  • Up-Regulation

Substances

  • Enzymes, Immobilized
  • Resins, Synthetic
  • Lipase
  • Ibuprofen