Open AccessCovalent Immobilization of Dehydrogenases on Carbon Felt for Reusable Anodes with Effective Electrochemical Cofactor Regeneration
Author(s) -
Pietricola Giuseppe,
Chamorro Lesly,
Castellino Micaela,
Maureira Diego,
Tommasi Tonia,
Hernández Simelys,
Wilson Lorena,
Fino Debora,
Ottone Carminna
Publication year - 2022
Publication title -
chemistryopen
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.644
H-Index - 29
ISSN - 2191-1363
DOI - 10.1002/open.202200102
Subject(s) - formate dehydrogenase , cofactor , chemistry , alcohol dehydrogenase , electrochemistry , formate , nicotinamide adenine dinucleotide , nad+ kinase , combinatorial chemistry , electrode , organic chemistry , inorganic chemistry , catalysis , ethanol , enzyme
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.