KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM Candida antarctica B

Authors

  • Jenifer CRUZ
  • Rodrigo TORRES
  • Claudia ORTIZ

Keywords:

Lipases, biotransformation, protein engineering, immobilized enzymes.

Abstract


The development of methodologies for obtaining chiral compounds constitutes a major challenge on current chemistry. In this context, kinetic resolution catalyzed by lipases represents an excellent alternative. In homogeneous media, these enzymes display an equilibrium between two conformations (open and closed form), that can be displaced towards an open conformation (active form) in presence of hydrophobic supports. In this article lipase from Candida antarctica B (CAL-B) was purified and covalently immobilized onto Eupergit C epoxy supports (EC), Eupergit C activated with other functional groups and octyl-agarose supports. These preparations of immobilized enzymes were used under different pH conditions in the kinetic resolution of (R,S)-methyl mandelate. In this study, EC-amino-CAL-B immobilized derivative was highlighted because it is highly enantioselective at pH 8 (enantiomeric ratio (E) of 52), allowing to obtain an R-enantiomer from mandelic acid with an enantiomeric excess (ee) of 96%.
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Published

2011-05-17

How to Cite

CRUZ, J., TORRES, R., & ORTIZ, C. (2011). KINETIC RESOLUTION OF (R,S)-METHYL MANDELATE BY IMMOBILIZED LIPASE PREPARATIONS FROM <I>Candida antarctica</I> B. Vitae, 18(1), 33–41. Retrieved from https://revistas.udea.edu.co/index.php/vitae/article/view/8775

Issue

Section

Biotechnology