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Covalent Immobilization of Dehydrogenases on Carbon Felt for Reusable Anodes with Effective Electrochemical Cofactor Regeneration
This study presents the immobilization with aldehyde groups (glyoxyl carbon felt) of alcohol dehydrogenase (ADH) and formate dehydrogenase (FDH) on carbon‐felt‐based electrodes. The compatibility of the immobilization method with the electrochemical application was studied with the ADH bioelectrode....
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9630042/ https://www.ncbi.nlm.nih.gov/pubmed/35856864 http://dx.doi.org/10.1002/open.202200102 |
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author | Pietricola, Giuseppe Chamorro, Lesly Castellino, Micaela Maureira, Diego Tommasi, Tonia Hernández, Simelys Wilson, Lorena Fino, Debora Ottone, Carminna |
author_facet | Pietricola, Giuseppe Chamorro, Lesly Castellino, Micaela Maureira, Diego Tommasi, Tonia Hernández, Simelys Wilson, Lorena Fino, Debora Ottone, Carminna |
author_sort | Pietricola, Giuseppe |
collection | PubMed |
description | This study presents the immobilization with aldehyde groups (glyoxyl carbon felt) of alcohol dehydrogenase (ADH) and formate dehydrogenase (FDH) on carbon‐felt‐based electrodes. The compatibility of the immobilization method with the electrochemical application was studied with the ADH bioelectrode. The electrochemical regeneration process of nicotinamide adenine dinucleotide in its oxidized form (NAD(+)), on a carbon felt surface, has been deeply studied with tests performed at different electrical potentials. By applying a potential of 0.4 V versus Ag/AgCl electrode, a good compromise between NAD(+) regeneration and energy consumption was observed. The effectiveness of the regeneration of NAD(+) was confirmed by electrochemical oxidation of ethanol catalyzed by ADH in the presence of NADH, which is the no active form of the cofactor for this reaction. Good reusability was observed by using ADH immobilized on glyoxyl functionalized carbon felt with a residual activity higher than 60 % after 3 batches. |
format | Online Article Text |
id | pubmed-9630042 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-96300422022-11-07 Covalent Immobilization of Dehydrogenases on Carbon Felt for Reusable Anodes with Effective Electrochemical Cofactor Regeneration Pietricola, Giuseppe Chamorro, Lesly Castellino, Micaela Maureira, Diego Tommasi, Tonia Hernández, Simelys Wilson, Lorena Fino, Debora Ottone, Carminna ChemistryOpen Research Articles This study presents the immobilization with aldehyde groups (glyoxyl carbon felt) of alcohol dehydrogenase (ADH) and formate dehydrogenase (FDH) on carbon‐felt‐based electrodes. The compatibility of the immobilization method with the electrochemical application was studied with the ADH bioelectrode. The electrochemical regeneration process of nicotinamide adenine dinucleotide in its oxidized form (NAD(+)), on a carbon felt surface, has been deeply studied with tests performed at different electrical potentials. By applying a potential of 0.4 V versus Ag/AgCl electrode, a good compromise between NAD(+) regeneration and energy consumption was observed. The effectiveness of the regeneration of NAD(+) was confirmed by electrochemical oxidation of ethanol catalyzed by ADH in the presence of NADH, which is the no active form of the cofactor for this reaction. Good reusability was observed by using ADH immobilized on glyoxyl functionalized carbon felt with a residual activity higher than 60 % after 3 batches. John Wiley and Sons Inc. 2022-07-20 /pmc/articles/PMC9630042/ /pubmed/35856864 http://dx.doi.org/10.1002/open.202200102 Text en © 2022 The Authors. Published by Wiley-VCH GmbH https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
spellingShingle | Research Articles Pietricola, Giuseppe Chamorro, Lesly Castellino, Micaela Maureira, Diego Tommasi, Tonia Hernández, Simelys Wilson, Lorena Fino, Debora Ottone, Carminna Covalent Immobilization of Dehydrogenases on Carbon Felt for Reusable Anodes with Effective Electrochemical Cofactor Regeneration |
title | Covalent Immobilization of Dehydrogenases on Carbon Felt for Reusable Anodes with Effective Electrochemical Cofactor Regeneration |
title_full | Covalent Immobilization of Dehydrogenases on Carbon Felt for Reusable Anodes with Effective Electrochemical Cofactor Regeneration |
title_fullStr | Covalent Immobilization of Dehydrogenases on Carbon Felt for Reusable Anodes with Effective Electrochemical Cofactor Regeneration |
title_full_unstemmed | Covalent Immobilization of Dehydrogenases on Carbon Felt for Reusable Anodes with Effective Electrochemical Cofactor Regeneration |
title_short | Covalent Immobilization of Dehydrogenases on Carbon Felt for Reusable Anodes with Effective Electrochemical Cofactor Regeneration |
title_sort | covalent immobilization of dehydrogenases on carbon felt for reusable anodes with effective electrochemical cofactor regeneration |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9630042/ https://www.ncbi.nlm.nih.gov/pubmed/35856864 http://dx.doi.org/10.1002/open.202200102 |
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