Abstract
Recent concerns over climate change have triggered many efforts to mitigate atmospheric CO2 levels. Among the CO2 utilization strategies, we, herein, aimed to biochemically characterize formate dehydrogenase from Clostridium ljungdahlii (ClFDH) for bioconversion of CO2 to versatile formate. ClFDH was functionally expressed in Escherichia coli without any accessory proteins and recombinant ClFDH were successfully characterized as CO2 reductase with a specific activity of 9.1 mU mg−1 for CO2 reduction. Additionally, the optimum pH was determined at pH 7.0 and 9.0 for CO2 reduction and formate oxidation, respectively. In particular, ClFDH retain its catalytic activity under aerobic conditions, even if C. ljungdahlii is a representative strict anaerobic microorganism. The results discussed herein would not only contribute to broaden biological routes for CO2 utilization but also provide significant insight into the valorization of CO2-containing industrial waste gases to value-added chemicals.
Published Version
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