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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
- Files in This Item:
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