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Bioelectrochemical conversion of CO2 to value added product formate using engineered Methylobacterium extorquens.
Jang, Jungho; Jeon, Byoung Wook; Kim, Yong Hwan.
Affiliation
  • Jang J; School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), 50 UNIST-gil, Ulsan, 44919, Republic of Korea.
  • Jeon BW; School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), 50 UNIST-gil, Ulsan, 44919, Republic of Korea.
  • Kim YH; School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), 50 UNIST-gil, Ulsan, 44919, Republic of Korea. metalkim@unist.ac.kr.
Sci Rep ; 8(1): 7211, 2018 05 08.
Article in En | MEDLINE | ID: mdl-29739951
ABSTRACT
The conversion of carbon dioxide to formate is a fundamental step for building C1 chemical platforms. Methylobacterium extorquens AM1 was reported to show remarkable activity converting carbon dioxide into formate. Formate dehydrogenase 1 from M. extorquens AM1 (MeFDH1) was verified as the key responsible enzyme for the conversion of carbon dioxide to formate in this study. Using a 2% methanol concentration for induction, microbial harboring the recombinant MeFDH1 expressing plasmid produced the highest concentration of formate (26.6 mM within 21 hours) in electrochemical reactor. 60 µM of sodium tungstate in the culture medium was optimal for the expression of recombinant MeFDH1 and production of formate (25.7 mM within 21 hours). The recombinant MeFDH1 expressing cells showed maximum formate productivity of 2.53 mM/g-wet cell/hr, which was 2.5 times greater than that of wild type. Thus, M. extorquens AM1 was successfully engineered by expressing MeFDH1 as recombinant enzyme to elevate the production of formate from CO2 after elucidating key responsible enzyme for the conversion of CO2 to formate.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Carbon Dioxide / Methylobacterium extorquens / Biocatalysis / Formate Dehydrogenases / Formates Language: En Journal: Sci Rep Year: 2018 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Carbon Dioxide / Methylobacterium extorquens / Biocatalysis / Formate Dehydrogenases / Formates Language: En Journal: Sci Rep Year: 2018 Document type: Article
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