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

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• 作者：Deniz Yildirim  ; ;   ; ^{dozyildirim@gmail.com} ; S. Seyhan Tü ; kel ; Dilek Alagö ; z ; Ö ; zlem Alptekin
• 关键词：Epoxide hydrolase ; Eupergit ; Kinetic resolution ; Racemic styrene oxide
• 刊名：Enzyme and Microbial Technology
• 出版年：2011
• 出版时间：10 December 2011
• 年：2011
• 卷：49
• 期：6-7
• 页码：555-559
• 全文大小：377 K

文摘

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 ¦Ìmol/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 ¡ãC. The free epoxide hydrolase retained 52 and 33 % of its maximum activity at 40 and 60 ¡ãC, 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.