详细信息

Confining Enzyme Clusters in Bacteriophage P22 Enhances Cofactor Recycling and Stereoselectivity for Chiral Alcohol Synthesis  ( SCI-EXPANDED收录 EI收录)  

文献类型:期刊文献

英文题名:Confining Enzyme Clusters in Bacteriophage P22 Enhances Cofactor Recycling and Stereoselectivity for Chiral Alcohol Synthesis

作者:Zhang, Yan-Qing[1];Feng, Tao-Tao[1];Cao, Yu-Fei[2,3,4];Zhang, Xiao-Yan[1];Wang, Tao[1];Nina, Mario Roque Huanca;Wang, Li-Cheng[5];Yu, Hui-Lei[1];Xu, Jian-He[1];Ge, Jun[2,3,4];Bai, Yun-Peng[1]

机构:[1]East China Univ Sci & Technol ECUST, Shanghai Collaborat Innovat Ctr Biomfg, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Tsinghua Univ, Minist Educ, Dept Chem Engn, Key Lab Ind Biocatalysis, Beijing 100084, Peoples R China;[3]Tsinghua Shenzhen Int Grad Sch, Inst Biopharmaceut & Hlth Engn, Shenzhen 518055, Peoples R China;[4]Shenzhen Bay Lab, Inst Biomed Hlth Technol & Engn, Shenzhen 518000, Peoples R China;[5]Tsinghua Univ, Dept Chem Engn, Minist Educ, Key Lab Ind Biocatalysis, Beijing 100084, Peoples R China

年份:2021

卷号:11

期号:16

起止页码:10487

外文期刊名:ACS CATALYSIS

收录:;EI(收录号:20213510835640);WOS:【SCI-EXPANDED(收录号:WOS:000687845800042)】;

基金:This work was financially sponsored by the National Key Research and Development Program of China (grant nos. 2 0 1 6 Y F A 0 2 0 4 3 0 0, 2 0 1 9Y F A 09 0 0 5 0 0 0, a n d 2018YFC1706200), the National Natural Science Foundation of China (grant nos. 22078096, 21536004, and 21871085), the Key Project of the Shanghai Science and Technology Committee (grant no. 18DZ1112703), and the Natural Science Foundation of Shanghai (grant no. 18ZR1409900).

语种:英文

外文关键词:enzyme cluster; enzymatic catalysis; cofactor recycling; confinement effects; asymmetric reduction

摘要:Cofactor recycling is important in the synthesis of chiral alcohols via bioreduction of ketones. Herein, a carbonyl reductase from Schef fersomyces stipitis (SsCR) and a glucose dehydrogenase from Bacillus megaterium (BmGDH) were confined in bacteriophage P22 nanoparticles. The recycling efficiency of nicotinamide adenine dinucleotide phosphate (NADPH) in these nanoparticles was enhanced by a factor of from 3 to 45 compared with the free enzyme system, which is attributed to the higher local concentrations of NADPH resulting from the confinement of the enzymes in the P22 nanoparticles. The consumption of NADPH can be reduced by an order of magnitude in scale-up synthesis compared with a free enzyme system.

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