Sustainable production of formic acid from CO2 by a novel immobilized mutant formate dehydrogenase

Renewable Hydrogen Production and Storage Via Enzymatic Interconversion of CO2 and Formate with Electrochemical Cofactor Regeneration

“…The potential effect of the mutation on the protein structure was initially investigated with molecular dynamics. The obtained mutant showed an almost 3‐fold higher k cat (0.42 s −1 as opposed to 0.16 s −1 for the wildtype) and lower K m (0.91 mM as opposed to 2.71 mM) for bicarbonate reduction in the presence of NADH at optimum pH 8 [153] . Moreover, mutants of EcFDH with improved stability have been investigated.…”

“…The obtained mutant showed an almost 3-fold higher k cat (0.42 s À 1 as opposed to 0.16 s À 1 for the wildtype) and lower K m (0.91 mM as opposed to 2.71 mM) for bicarbonate reduction in the presence of NADH at optimum pH 8. [153] Moreover, mutants of EcFDH with improved stability have been investigated. In particular, a rationally designed mutant with modified surface (occurring by replacing hydrophobic surface residues Tyr3, Phe26, Ile140 and Glu190 with hydrophilic Glu, Ser, Arg and Lys respectively) and additional salt bridges (created by substitution of Ser5 and Ile163 with Lys, Val168 and Gln70 with Asp, Leu150 with Arg and Leu155 with Glu), showed improved formate production rates, although no kinetic constants were calculated and hydrogenase and H 2 were also present in the reaction.…”

Engineering of formate dehydrogenase for improving conversion potential of carbon dioxide to formate

“…Among them, the V354G/F285W and V328I/F285W mutants demonstrated 2.2-and 2.6-fold improvement compared with its template CbFDH M2 in the preliminary screening by high throughput screening method. In order to further improve the catalysis capacity, enzyme immobilization strategy should be utilized in the following study (Tülek et al 2023).…”

“…In recent years, it has been reported that some formate dehydrogenases, especially NAD(P) + / metal cofactor dependent formate dehydrogenases, can reversibly reduce CO 2 to formate and thus act as non-photosynthetic CO 2 reductases (Du et al 2022;Liao et al 2022; Obert and Dave 1999; Wu et al 2023), but the catalytic activity towards CO 2 is relatively low. In order to improve the catalytic activity of reducing CO 2 to formate, protein engineering and immobilization strategy had been carried out (Bernal et al 2018;Tülek et al 2023).…”

Real flue gas CO2 hydrogenation to formate by an enzymatic reactor using O2- and CO-tolerant hydrogenase and formate dehydrogenase

“…FDHs are classified as metal-independent or metal-dependent based on the active site (molybdenum or tungsten) (Ünlü et al, 2021; Alpdağtaş et al, 2022). Although metal-independent FDH exhibits O 2 -independent activity, the strategies like mutation and immobilization have been reported to enhance its activity and stability due to its inherently low activity ( Çakar et al, 2020 ; Tülek et al, 2023 ). FDHs from Clostridium carb oxidovorans strain P7T ( Alissandratos et al, 2013 ), Chaetomium thermophilum ( Çakar et al, 2020 ), Rhodobacter capsulatus ( Hartmann and Leimkühler, 2013 ), and Methylobacterium extorquens AM1 ( Laukel et al, 2003 ) have maintained high CO 2 reduction activity under oxic conditions.…”