Insights into Cell-Free Conversion of CO2 to Chemicals by a Multienzyme Cascade Reaction

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Multienzymatic cascade reactions have garnered the attention of many researchers as an approach for converting CO, into methanol. The cascade reaction used in this study includes the following enzymes: a formate dehydrogenase (CIFDH), 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 CIFDH-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 (K-d and Delta G) 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.
Publisher
AMER CHEMICAL SOC
Issue Date
2018-12
Language
English
Article Type
Article
Citation

ACS CATALYSIS, v.8, no.12, pp.11085 - 11093

ISSN
2155-5435
DOI
10.1021/acscatal.8b02646
URI
http://hdl.handle.net/10203/250137
Appears in Collection
BS-Journal Papers(저널논문)
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