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Min Ji KIM,Stacy Simai REGINALD,Hyeryeong LEE,Serah CHOI,Basit SHARIF,In Seop CHANG 한국생물공학회 2021 한국생물공학회 학술대회 Vol.2021 No.10
Over the last century, the accumulation of carbon dioxide (CO₂) which accounts for the largest portion of greenhouse gases in the atmosphere has provoked extreme global warming and environmental issues. To tackle these issues, carbon capture, utilization and storage (CCUS) technology has received considerable attention through all the related areas. In the field of CO₂ conversion having an effect on CO₂ valorization to valuable chemicals as well as removal, biocatalysts such as enzyme are promising due to their high specificity to substrate and ability of catalysis at mild conditions. Herein, we focused on CO₂ reducing enzyme, formate dehydrogenase (EC 1.17.1.9) (FDH) which can reversibly catalyze CO₂ reduction and formate oxidation. FDHs existed in a diverse array of organisms can be divided into NAD⁺-dependent and metal-dependent FDH. While metal-dependent FDH is highly efficient for CO₂ reduction to formate but requires strict anaerobic conditions, NAD⁺-dependent FDH can be easily handled, but NADH are required as a natural cofactor. In this study, we attempted to investigate the availability of Candida methylica FDH(cmFDH) for electroenzymatic CO₂ reduction to formate. Solid-binding peptide (SBP) was introduced at either N- terminus (gbp(N)-FDH) or C- terminus (FDH-gbp(C)) via protein engineering to develop a stable enzyme immobilization at the enzyme-electrode interface. The recombinant FDH and the two synthetic FDHs are characterized for their biocatalytic activity. The results indicated that GBP fusion CmFDHs retain or improve their enzyme activities. Cyclic voltammetry (CV) result shows that the electrons can be directly transferred from FDHs to the electrode surface and vice versa for formate oxidation and CO₂ reduction in the absence of NADH.