CO2 conversion into formate catalysed by immobilized formate dehydrogenases and regeneration of the NADH cofactor used during conversion

(2025) 15th European Congress of Chemical Engineering (ECCE) & 8th European Congress of Applied Biotechnology (ECAB) & 3rd Iberoamerica — Location: Lisbonne (8.September.2025)

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Abstract
Upgrading CO2 into a chemical compound is a way of moving towards carbon circularity. Formate is the first reduced form of CO2 and is the basis for the synthesis of many other molecules. Converting CO2 using enzymes enables higher conversion rates to be achieved at a lower environmental cost (Al-Tamreh et al., 2021). The method for converting CO2 into formate developed in this work is inspired by a known biochemical route consisting of a redox reaction between CO2 and NADH in the presence of formate dehydrogenases (FDH) as catalysts. NADH has a high economic cost, hence, it is necessary to regenerate it during the process. The aim of this work is therefore to develop and optimize a CO2 conversion and NADH regeneration route with minimal energy demand, cost and environmental impact. The conversion of CO2 into formate is catalyzed by FDHs that are immobilized on the membrane to increase their stability. A recent technique developed by our research team to immobilize enzymes, consisting of activating the PVDF membrane with chitosan, showed performance similar to that described in the literature (Guo et al., 2021), with an apparent specific activity of 0.02 mM/h/mg for the immobilized FDHs. The regeneration of NADH takes place via hydride exchange from a reducing agent through an ion exchange membrane. A deep study on potential reducing agents that could regenerate NADH was performed, finding other nicotinamides as very interesting redox couples. The first steps to develop a complete process for CO2 conversion and NADH regeneration is shown in this work, providing a continuous production of formate from CO2 from flue gases.
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Toussaint, Y., Luis Alconero, P., & et al. (2025). CO2 conversion into formate catalysed by immobilized formate dehydrogenases and regeneration of the NADH cofactor used during conversion. 15th European Congress of Chemical Engineering (ECCE) & 8th European Congress of Applied Biotechnology (ECAB) & 3rd Iberoamerica, Lisbonne. https://hdl.handle.net/2078.5/258533