详细信息
Coimmobilized Dual Enzymes in a Continuous Flow Reactor for the Efficient Synthesis of Optically Pure γ/δ-Lactones ( SCI-EXPANDED收录)
文献类型:期刊文献
英文题名:Coimmobilized Dual Enzymes in a Continuous Flow Reactor for the Efficient Synthesis of Optically Pure γ/δ-Lactones
作者:Yuan, Pengyu[1];Wang, Qing[1];Deng, Xuelei[1];Zhang, Xiaoyan[1];Fan, Daidi[2];Bai, Yunpeng[1,2]
机构:[1]East China Univ Sci & Technol, Shanghai Collaborat Innovat Ctr Biomfg, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Northwest Univ, Shaanxi R&D Ctr Biomat & Fermentat Engn, Sch Chem Engn, Xian 710069, Shaanxi, Peoples R China
年份:2024
卷号:17
期号:1
起止页码:867
外文期刊名:ACS APPLIED MATERIALS & INTERFACES
收录:;WOS:【SCI-EXPANDED(收录号:WOS:001379946400001)】;
基金:This work was financially sponsored by the National Key R&D Program of China (grant nos. 2021YFC2102800), the National Natural Science Foundation of China (grant nos. 22078096 and 22378120).
语种:英文
外文关键词:enzyme catalysis; enzyme immobilization; cofactorrecycling; continuous-flow; microreactor
摘要:Enzyme catalysis is a promising method for producing chiral chemicals with high stereoselectivity under mild conditions. However, the traditional batch reaction suffers from low enzyme stability, low cofactor recycling, and poor enzyme reusability. Here, we present a continuous-flow method using coimmobilized dual enzymes for the synthesis of chiral gamma-/delta-lactones, which are widely used in fragrances and flavors. Typically, a carbonyl reductase mutant SmCRM5 from Serratia marcescens, was coimmobilized by covalent binding with BmGDH, a glucose dehydrogenase capable of recovering and recycling the cofactor NADPH. After immobilization, SmCRM5 and BmGDH exhibited a 8.9-/8.7-fold increase in catalytic efficiency (k cat/K m) and a 57-/15-fold increase in half-life at 30 degrees C, respectively. We demonstrated that coimmobilized dual enzymes used in a continuous flow reactor showed a higher reaction rate and a higher space-time yield (1586 g
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