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Molecules 2020, 25, 3653 13 of 23 The combination of photocatalysis and biocatalysis showed higher efficiency in CO2 reduction than that of photocatalysis. However, the prominent problem is the interference between the photocatalysis and biocatalysis, resulting in corrosion of the photocatalyst and inactivation of the enzyme. Additionally, the enzyme used in the biocatalysis is reversible and it is easy to perform the reverse reaction and charge reorganization [128]. To solve this problem, researchers adopted an electric field on the basis of photoenzymatic catalysis, which can effectively promote charge separation and improve the conversion efficiency of CO2. 2.7. Enzyme Coupled to Photoelectrocatalysis Photocatalysis and electrocatalysis are combined to form a photoelectric cooperative catalysis, and then combined with biocatalysis to form a photoelectrochemical (PEC) cell similar to maintain the optimal conditions of enzymes and improve conversion efficiency [129,130]. Conducting wire was used to ensure the oriented transfer of reducing equivalents (primarily electrons, H+) from the photoelectrode to biocatalysis. Nam et al. [131] imagined that photoelectrochemical (PEC) cells could inhibit biocatalytic charge recombination and reverse reactions because photocatalytic and biocatalytic reactions can be separated in the anode and cathode compartments, respectively. An anode compartment with cobalt phosphate (Co-Pi) deposited hematite (Fe2O3) photoanode for photocatalytic water oxidation and a cathode compartment with formate dehydrogenase for NADH regeneration and CO2 reduction were designed (Figure 8). The co-catalyst (Co-Pi) in the photoelectrode can reduce the activation energy quickly, improve the quantum efficiency by promoting charge separation, and consume the photogenerated charges in time to improve the stability of the photoelectrode [132]. As can be seen from Figure 8, the PEC system is divided into two compartments in which the oxidation reaction of water can be well separated from the enzymatic reaction. The two compartments do not affect each Molecules 2020, 25, x FOR PEER REVIEW 14 of 24 other, enabling the formate dehydrogenase to work at its optimal pH conditions. Figure 8. Schematic illustration of the biocatalytic PEC platform [131]. Figure 8. Schematic illustration of the biocatalytic PEC platform [131]. Generally, enzymes are easily affected by the reaction environment, making the enzyme electrode Generally, enzymes are easily affected by the reaction environment, making the enzyme unstable [133]. For example, the enzyme cannot perform its maximum activity at a non-optimal pH electrode unstable [133]. For example, the enzyme cannot perform its maximum activity at a non- solution. Eun-Gyu Choi and coauthors [134] studied the effect of pH on a coupled photoelectric–enzyme optimal pH solution. Eun-Gyu Choi and coauthors [134] studied the effect of pH on a coupled system. RcFDH-driven CO2 reduction was predominant at an acidic pH, whereas formate oxidation was photoelectric–enzyme system. RcFDH-driven CO2 reduction was predominant at an acidic pH, favorable at basic conditions. pH = 6.5 is the most suitable condition for CO2 reduction to formic acid whereas formate oxidation was favorable at basic conditions. pH = 6.5 is the most suitable condition in their photoenzyme system by the comparison of the results at different pH values. For the stability for CO2 reduction to formic acid in their photoenzyme system by the comparison of the results at and reusability of the enzyme, appropriate fixation methods can be adopted. Lee et al. [112] reported different pH values. For the stability and reusability of the enzyme, appropriate fixation methods can that a tightly organized biophotocathode (EC-PDA)-electrochemically synthesized polydopamine be adopted. Lee et al. [112] reported that a tightly organized biophotocathode (EC-PDA)- (PDA) film was copolymerized with FDH (E) and NADH (C) in which CO2 can be reduced to formic electrochemically synthesized polydopamine (PDA) film was copolymerized with FDH (E) and acid with high selectivity. The PDA was chosen as the substrate for enzyme immobilization because NADH (C) in which CO2 can be reduced to formic acid with high selectivity. The PDA was chosen as the substrate for enzyme immobilization because of its excellent biocompatibility and charge transfer ability [135]. The PDA layer on the electrode can fulfill the requirement of electron transfer and enzyme stabilization and extend the service life of the enzyme [136]. A similar photoelectrochemical cell was constructed by the EC-incorporated PDA bioelectrode and cobalt phosphate/bismuth vanadate (CoPi/BiVO4) photoanode by which the reduction of CO2 can be achieved without externalPDF Image | Research Progress in Conversion of CO2 to Valuable Fuels
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