Preparative-scale kinetic resolution of racemic styrene oxide by immobilized epoxide hydrolase


YILDIRIM D. , TÜKEL S. S. , ALAGÖZ D. , ALPTEKİN Ö.

ENZYME AND MICROBIAL TECHNOLOGY, cilt.49, ss.555-559, 2011 (SCI İndekslerine Giren Dergi) identifier identifier identifier

  • Cilt numarası: 49
  • Basım Tarihi: 2011
  • Doi Numarası: 10.1016/j.enzmictec.2011.08.003
  • Dergi Adı: ENZYME AND MICROBIAL TECHNOLOGY
  • Sayfa Sayıları: ss.555-559

Özet

Epoxide hydrolase from Aspergillus niger was immobilized onto the modified Eupergit C 250 L through a Schiff base formation. Eupergit C 250 L was treated with ethylenediamine to introduce primary amine groups which were subsequently activated with glutaraldehyde. The amount of introduced primary amine groups was 220 mu mol/g of the support after ethylenediamine treatment, and 90% of these groups were activated with glutaraldehyde. Maximum immobilization of 80% was obtained with modified Eupergit C 250 L under the optimized conditions. The optimum pH was 7.0 for the free epoxide hydrolase and 6.5 for the immobilized epoxide hydrolase. The optimum temperature for both free and immobilized epoxide hydrolase was 40 degrees C. The free epoxide hydrolase retained 52 and 33% of its maximum activity at 40 and 60 degrees C, respectively after 24 h preincubation time whereas the retained activities of immobilized epoxide hydrolase at the same conditions were 90 and 75%, respectively. Immobilized epoxide hydrolase showed about 2.5-fold higher enantioselectivity than that of free epoxide hydrolase. A preparative-scale (120 g/L) kinetic resolution of racemic styrene oxide using immobilized preparation was performed in a batch reactor and (S)-styrene oxide and (R)-1-phenyl-1,2-ethanediol were both obtained with about 50% yield and 99% enantiomeric excess. The immobilized epoxide hydrolase was retained 90% of its initial activity after 5 reuses. (C) 2011 Elsevier Inc. All rights reserved.