Effect of confinement of horse heart cytochrome c and formate dehydrogenase from Candida boidinii on mesoporous carbons on their catalytic activity
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Título: | Effect of confinement of horse heart cytochrome c and formate dehydrogenase from Candida boidinii on mesoporous carbons on their catalytic activity |
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Autor/es: | Hernández Ibáñez, Naiara | Montiel, Vicente | Gomis-Berenguer, Alicia | Ania, Conchi O. | Iniesta, Jesus |
Grupo/s de investigación o GITE: | Electroquímica Aplicada y Electrocatálisis |
Centro, Departamento o Servicio: | Universidad de Alicante. Departamento de Química Física | Universidad de Alicante. Instituto Universitario de Electroquímica |
Palabras clave: | Mesoporous carbon | Protein nanoconfinement | Cytochrome c | Formate dehydrogenase hydrogen peroxide | Carbon dioxide |
Área/s de conocimiento: | Química Física |
Fecha de publicación: | 3-abr-2021 |
Editor: | Springer Nature |
Cita bibliográfica: | Bioprocess and Biosystems Engineering. 2021, 44: 1699-1710. https://doi.org/10.1007/s00449-021-02553-3 |
Resumen: | This study reports the immobilization of two biocatalysts (e.g., cytochrome c—Cyt c—and the non-metalloenzyme formate dehydrogenase from Candida boidinii–cbFDH) on a series of mesoporous carbons with controlled pore sizes. The catalytic activity of the nanoconfined proteins was correlated with the pore size distribution of the carbon materials used as supports. The electrochemical behaviour of nanoconfined Cyt c showed direct electron transfer electroactivity in pore sizes matching tightly the protein dimension. The pseudo-peroxidase activity towards H2O2 reduction was enhanced at pH 4.0, due to the protein conformational changes. For cbFDH, the reduction of CO2 towards formic acid was evaluated for the nanoconfined protein, in the presence of nicotinamide adenine dinucleotide (NADH). The carbons displayed different cbFDH uptake capacity, governed by the dimensions of the main mesopore cavities and their accessibility through narrow pore necks. The catalytic activity of nanoconfined cbFDH was largely improved, compared to its performance in free solution. Regardless of the carbon support used, the production of formic acid was higher upon immobilization with lower nominal cbFDH:NADH ratios. |
Patrocinador/es: | NHI. VM and JI thank MINICINN, Spain (projects CTQ2013-48280-C3-3-R and CTQ2016-76231-C2-2-R) for financial support. COA thanks the financial support of the European Research Council through a Consolidator Grant (PHOROSOL 684161). |
URI: | http://hdl.handle.net/10045/114070 |
ISSN: | 1615-7591 (Print) | 1615-7605 (Online) |
DOI: | 10.1007/s00449-021-02553-3 |
Idioma: | eng |
Tipo: | info:eu-repo/semantics/article |
Derechos: | © The Author(s) 2021. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
Revisión científica: | si |
Versión del editor: | https://doi.org/10.1007/s00449-021-02553-3 |
Aparece en las colecciones: | INV - LEQA - Artículos de Revistas |
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