Fabrication of a biocathode for formic acid production upon the immobilization of formate dehydrogenase from Candida boidinii on a nanoporous carbon
| Autor: | Conchi O. Ania, Jesús Iniesta, Vicente Montiel, Naiara Hernández-Ibáñez, Alicia Gomis-Berenguer |
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| Přispěvatelé: | Universidad de Alicante. Departamento de Química Física, Universidad de Alicante. Instituto Universitario de Electroquímica, Electroquímica Aplicada y Electrocatálisis |
| Rok vydání: | 2021 |
| Předmět: |
Formate dehydrogenase from Candida boidinii
Environmental Engineering Immobilized enzyme Formates Formic acid Health Toxicology and Mutagenesis chemistry.chemical_element Electrosynthesis Formate dehydrogenase Cofactor chemistry.chemical_compound Nanopores Nafion Electrochemical regeneration Environmental Chemistry Química Física biology Formic acid NADH-Regeneration Public Health Environmental and Occupational Health General Medicine General Chemistry Carbon Dioxide Pollution Formate Dehydrogenases Carbon chemistry Saccharomycetales biology.protein Biocathode Mesoporous carbon Nuclear chemistry |
| Zdroj: | Chemosphere RUA. Repositorio Institucional de la Universidad de Alicante Universidad de Alicante (UA) |
| ISSN: | 1879-1298 |
| Popis: | The immobilization of the non-metallic enzyme formate dehydrogenase from Candida boidinii (CbFDH) into a nanoporous carbon with appropriate pore structure was explored for the bioelectrochemical conversion of CO2 to formic acid (FA). Higher FA production rates were obtained upon immobilization of CbFDH compared to the performance of the enzyme in solution, despite the lower nominal CbFDH to NADH (β-nicotinamide adenine dinucleotide reduced) cofactor ratio and the lower amount of enzyme immobilized. The co-immobilization of the enzyme and a rhodium complex as mediator in the nanoporous carbon allowed the electrochemical regeneration of the cofactor. Preparative electrosynthesis of FA carried out on biocathodes of relatively large dimensions (ca. 3 cm × 2 cm) confirmed the higher production rate of FA for the immobilized enzyme. Furthermore, the incorporation of a Nafion binder in the biocathodes did not modify the immobilization extent of the CbFDH in the carbon support. Coulombic efficiencies close to 46% were obtained for the electrosynthesis carried out at −0.8 V for the biocathodes prepared using the lowest Nafion binder content and the co-immobilized enzyme and rhodium redox mediator. Although these values may yet be improved, they confirm the feasibility of these biocathodes in larger scales (6 cm2) beyond most common electrode dimensions reported in the literature (ca. a few mm2). NH, VM and JI thank Spanish MINICINN (projects CTQ2016-76231-C2-2-R and PID2019-108136RB-C32) for financial support. COA thanks the financial support of the European Research Council through a Consolidator Grant (PHOROSOL 684161). |
| Databáze: | OpenAIRE |
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