文献类型：期刊文献

英文题名：One-pot biocatalytic route from cycloalkanes to α,ω-dicarboxylic acids by designed Escherichia coli consortia

作者：Wang, Fei[1];Zhao, Jing[1];Li, Qian[1];Yang, Jun[1];Li, Renjie[1];Min, Jian[1];Yu, Xiaojuan[1];Zheng, Gao-Wei[2,3];Yu, Hui-Lei[2,3];Zhai, Chao[1];Acevedo-Rocha, Carlos G.[4];Ma, Lixin[1];Li, Aitao[1]

机构：[1]Hubei Univ, State Key Lab Biocatalysis & Enzyme Engn, Hubei Collaborat Innovat Ctr Green Transformat Bi, Hubei Key Lab Ind Biotechnol,Sch Life Sci, Wuhan 430062, Peoples R China;[2]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[3]East China Univ Sci & Technol, Shanghai Collaborat Innovat Ctr Biomfg, Shanghai 200237, Peoples R China;[4]Biosyntia ApS, DK-2100 Copenhagen, Denmark

年份：2020

卷号：11

期号：1

外文期刊名：NATURE COMMUNICATIONS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000577244600001)】；

基金：This study was supported by the National Key Research and Development Program of China (2019YFA09005000), by the National Natural Science Foundation of China (No. 21977026 and 21702052) and Research Program of State Key Laboratory of Biocatalysis and Enzyme Engineering.

语种：英文

摘要：Aliphatic alpha,omega-dicarboxylic acids (DCAs) are a class of useful chemicals that are currently produced by energy-intensive, multistage chemical oxidations that are hazardous to the environment. Therefore, the development of environmentally friendly, safe, neutral routes to DCAs is important. We report an in vivo artificially designed biocatalytic cascade process for biotransformation of cycloalkanes to DCAs. To reduce protein expression burden and redox constraints caused by multi-enzyme expression in a single microbe, the biocatalytic pathway is divided into three basic Escherichia coli cell modules. The modules possess either redox-neutral or redox-regeneration systems and are combined to form E. coli consortia for use in biotransformations. The designed consortia of E. coli containing the modules efficiently convert cycloalkanes or cycloalkanols to DCAs without addition of exogenous coenzymes. Thus, this developed biocatalytic process provides a promising alternative to the current industrial process for manufacturing DCAs.