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The enzymatic electrosynthesis of formic acid from the reduction of carbon dioxide (CO2) by using formate dehydrogenase (FDH) as a catalyst at the cathode in both its free and immobilized forms was studied in detail in a bioelectrochemical system (BES). The essential role of solubilizing CO2 for its conversion was also studied by adding carbonic anhydrase (CA) to the FDH enzyme in both its free and immobilized forms. FDH alone in the free form showed large variation in the reduction current [(−6.2±3.9) A m−2], whereas the immobilized form showed less variation [(−3.8±0.5) A m−2] due to increased enzyme stability. The addition of CA with FDH increased the consumption of the current in both forms due to the fact that it allowed rapid dissolution of CO2, which made it available for the catalytic reaction with FDH. Remarkably, stable consumption of the current was observed throughout the operation if both CA and FDH were immobilized onto the electrode [(−3.9±0.2) A m−2]. Product formation by the immobilized enzyme was also continued for three repetitive cycles, which revealed the longevity of the enzyme after immobilization. The recyclability of NADH (NAD=nicotinamide adenine dinucleotide) was also clearly evidenced on the derivative voltammetric signature. Extension of this study for continuous and long‐term operation may reveal more possibilities for the rapid capture and conversion of CO2.

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