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In situ modulation of enzyme activity via heterogeneous catalysis utilizing solid electroplated cofactors

During product isolation the received bioreceptors often do not exhibit a sufficient biochemical activity due to multistep dissociation and loss of cofactors. However, for bioelectrochemical applications the presence of cofactors is necessary for a successful oxidative or reductive conversion of the...

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Autores principales: Apushkinskaya, N., Zolotukhina, E.V., Butyrskaya, E.V., Silina, Y.E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9307585/
https://www.ncbi.nlm.nih.gov/pubmed/35891780
http://dx.doi.org/10.1016/j.csbj.2022.07.012
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author Apushkinskaya, N.
Zolotukhina, E.V.
Butyrskaya, E.V.
Silina, Y.E.
author_facet Apushkinskaya, N.
Zolotukhina, E.V.
Butyrskaya, E.V.
Silina, Y.E.
author_sort Apushkinskaya, N.
collection PubMed
description During product isolation the received bioreceptors often do not exhibit a sufficient biochemical activity due to multistep dissociation and loss of cofactors. However, for bioelectrochemical applications the presence of cofactors is necessary for a successful oxidative or reductive conversion of the substrates to the products. Herein, we show how the immobilization of the required electroplated cofactors in a design of amperometric electrodes can in situ assist the activity of apo-enzymes. Compared to conventional approaches used in enzyme engineering this tailored nanoengineering methodology is superior from economic point of view, labor and time costs, storage conditions, reduced amount of waste and can fill the gap in the development of tuned bioelectrocatalysts.
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spelling pubmed-93075852022-07-25 In situ modulation of enzyme activity via heterogeneous catalysis utilizing solid electroplated cofactors Apushkinskaya, N. Zolotukhina, E.V. Butyrskaya, E.V. Silina, Y.E. Comput Struct Biotechnol J Communications During product isolation the received bioreceptors often do not exhibit a sufficient biochemical activity due to multistep dissociation and loss of cofactors. However, for bioelectrochemical applications the presence of cofactors is necessary for a successful oxidative or reductive conversion of the substrates to the products. Herein, we show how the immobilization of the required electroplated cofactors in a design of amperometric electrodes can in situ assist the activity of apo-enzymes. Compared to conventional approaches used in enzyme engineering this tailored nanoengineering methodology is superior from economic point of view, labor and time costs, storage conditions, reduced amount of waste and can fill the gap in the development of tuned bioelectrocatalysts. Research Network of Computational and Structural Biotechnology 2022-07-12 /pmc/articles/PMC9307585/ /pubmed/35891780 http://dx.doi.org/10.1016/j.csbj.2022.07.012 Text en © 2022 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Communications
Apushkinskaya, N.
Zolotukhina, E.V.
Butyrskaya, E.V.
Silina, Y.E.
In situ modulation of enzyme activity via heterogeneous catalysis utilizing solid electroplated cofactors
title In situ modulation of enzyme activity via heterogeneous catalysis utilizing solid electroplated cofactors
title_full In situ modulation of enzyme activity via heterogeneous catalysis utilizing solid electroplated cofactors
title_fullStr In situ modulation of enzyme activity via heterogeneous catalysis utilizing solid electroplated cofactors
title_full_unstemmed In situ modulation of enzyme activity via heterogeneous catalysis utilizing solid electroplated cofactors
title_short In situ modulation of enzyme activity via heterogeneous catalysis utilizing solid electroplated cofactors
title_sort in situ modulation of enzyme activity via heterogeneous catalysis utilizing solid electroplated cofactors
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9307585/
https://www.ncbi.nlm.nih.gov/pubmed/35891780
http://dx.doi.org/10.1016/j.csbj.2022.07.012
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