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One-pot biocatalytic route from cycloalkanes to ?,?-dicarboxylic acids by designed Escherichia coli consortia.


ABSTRACT: Aliphatic ?,?-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.

SUBMITTER: Wang F 

PROVIDER: S-EPMC7542165 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

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One-pot biocatalytic route from cycloalkanes to α,ω-dicarboxylic acids by designed Escherichia coli consortia.

Wang Fei F   Zhao Jing J   Li Qian Q   Yang Jun J   Li Renjie R   Min Jian J   Yu Xiaojuan X   Zheng Gao-Wei GW   Yu Hui-Lei HL   Zhai Chao C   Acevedo-Rocha Carlos G CG   Ma Lixin L   Li Aitao A  

Nature communications 20201007 1


Aliphatic α,ω-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  ...[more]

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