Insights into cell-free conversion of CO2 to chemicals by a multienzyme cascade reaction = 무세포 다중효소 연쇄반응을 통한 이산화탄소의 케미컬 전환

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Title
Insights into cell-free conversion of CO2 to chemicals by a multienzyme cascade reaction = 무세포 다중효소 연쇄반응을 통한 이산화탄소의 케미컬 전환
Author(s)
R K Singh; R Singh; D Sivakumar; S Kondaveeti; T Kim; J Li; Bong Hyun Sung; B K Cho; D R Kim; S C Kim; V C Kalia; Y H P J Zhang; H Zhao; Y C Kang; J K Lee
Bibliographic Citation
ACS Catalysis, vol. 8, pp. 11085-11093
Publication Year
2018
Abstract
Multienzymatic cascade reactions have garnered the attention of many researchers as an approach for converting CO2 into methanol. The cascade reaction used in this study includes the following enzymes: a formate dehydrogenase (ClFDH), a formaldehyde dehydrogenase (BmFaldDH), and an alcohol dehydrogenase (YADH) from Clostridium ljungdahlii, Burkholderia multivorans, and Saccharomyces cerevisiae, respectively. Because this cascade reaction requires NADH as a cofactor, phosphite dehydrogenase (PTDH) was employed to regenerate the cofactor. The multienzymatic cascade reaction, along with PTDH, yielded 3.28 mM methanol. The key to the success of this cascade reaction was a novel formaldehyde dehydrogenase, BmFaldDH, the enzyme catalyzing the reduction of formate to formaldehyde. The methanol yield was further improved by incorporation of 1-ethyl-3-methylimidazolium acetate (EMIM-Ac), resulting in 7.86 mM of methanol. A 500-fold increase in total turnover number was observed for the ClFDH-BmFaldDH-YADH cascade system compared to the Candida boidinii FDH-Pseudomonas putida FaldDH-YADH system. We provided detailed insights into the enzymatic reduction of CO2 by determining the thermodynamic parameters (Kd and ΔG) using isothermal titration calorimetry. Furthermore, we demonstrated a novel time-dependent formaldehyde production from CO2. Our results will aid in the understanding and development of a robust multienzyme catalyzed cascade reaction for the reduction of CO2 to value-added chemicals.
Keyword
cascade reactionCO2FaldDHformaldehydemethanolmultienzymeFDH
ISSN
2155-5435
Publisher
Amer Chem Soc
DOI
http://dx.doi.org/10.1021/acscatal.8b02646
Type
Article
Appears in Collections:
Synthetic Biology and Bioengineering Research Institute > Synthetic Biology Research Center > 1. Journal Articles
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