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纳米粒子固定化双酶耦合体系连续催化制备(R)-苯基乙二醇

  • 彭益强 张尧
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  • 华侨大学工业生物技术福建省高校重点实验室 华侨大学工业生物技术福建省高校重点实验室

收稿日期: 2015-10-21

  修回日期: 2015-11-30

  网络出版日期: 2016-12-22

Continuous Preparation of (R)-Phenyl-ethanediol by Catalysis of Nanoparticles Immobilized Bi-enzyme Coupling System

  • PENG Yi-qiang ZHANG Yao
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  • Provincial Key Laboratory of Industrial Biotechnology, Huaqiao University Provincial Key Laboratory of Industrial Biotechnology, Huaqiao University

Received date: 2015-10-21

  Revised date: 2015-11-30

  Online published: 2016-12-22

摘要

将活化醇盐水解法制备的SiO2纳米粒子分别与羰基还原酶(CR)和甲酸脱氢酶(FDH)进行共价固定化,固定化CR与FDH耦合,连续催化转化b-羟基苯乙酮制备(R)-苯基乙二醇,考察了NADH的再生与循环利用性. 结果表明,纳米粒子固定化CR和FDH酶载量分别为3.32和5.55 mg/g,催化活性为游离酶的50%~60%,最适反应pH值分别为6.5和8.5,最适反应温度分别为40和45℃. 耦合体系进行12批次反应,产物(R)-苯基乙二醇累积量达35.6 g/L,纳米粒子生产能力达178 g/g. 纳米粒子固定化酶经简单离心收集后可重复利用.

本文引用格式

彭益强 张尧 . 纳米粒子固定化双酶耦合体系连续催化制备(R)-苯基乙二醇[J]. 过程工程学报, 2016 , 16(2) : 286 -291 . DOI: 10.12034/j.issn.1009-606X.215361

Abstract

SiO2 nanoparticles prepared by the alkoxide hydrolysis precipitation method were covalently immobilized with carbonyl reductase (CR) and formate dehydrogenase (FDH). The nanopartiles immobilized CR and FDH were coupled and used for continuous catalytic conversion of β-hydroxyacetophenone to optical purity (R)-phenyl-ethanediol, and in situ NADH regeneration and recycling analyzed. The results showed that the enzyme loading of nanopartiles immobilized CR and FDH was 3.32 and 5.55 mg/g, their catalytic capability 50%~60% of native enzyme, their optimal reaction pH value 6.5 and 8.5, and their optimal reaction temperature 40 and 45℃, respectively. The production of (R)-phenyl-ethanediol was accumulated as 35.6 g/L, and the productivity of unit nanoparticles 178 g/g, while the coupling system was carried out for 12 batches. The nanopartiles immobilized CR and FDH could be reused after collection with centrifugal separation.
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