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

• Main Authors: Jenifer CRUZ, Rodrigo TORRES, Claudia ORTIZ
• Format: Article in Journal/Newspaper
• Language: English
• Published: Universidad de Antioquia 2011
• Subjects: Lipases; biotransformation; protein engineering; immobilized enzymes; Food processing and manufacture; TP368-456; Pharmaceutical industry; HD9665-9675; Antarc*; Antarctica
• Online Access: https://doaj.org/article/b8a5572b8874465abee176833b973d1c

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%.