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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....

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Autores principales: Pietricola, Giuseppe, Chamorro, Lesly, Castellino, Micaela, Maureira, Diego, Tommasi, Tonia, Hernández, Simelys, Wilson, Lorena, Fino, Debora, Ottone, Carminna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
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.
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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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