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Glucose oxidase converted into a general sugar-oxidase

Entrapment of glucose oxidase (GOx) within metallic gold converts this widely used enzyme into a general saccharide oxidase. The following sugar molecules were oxidized by the entrapped enzyme (in addition to d-glucose): fructose, xylose, l-glucose, glucose-6-phosphate, sucrose, lactose, methylgluco...

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Autores principales: Baruch-Shpigler, Yael, Avnir, David
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9226012/
https://www.ncbi.nlm.nih.gov/pubmed/35739181
http://dx.doi.org/10.1038/s41598-022-14957-6
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author Baruch-Shpigler, Yael
Avnir, David
author_facet Baruch-Shpigler, Yael
Avnir, David
author_sort Baruch-Shpigler, Yael
collection PubMed
description Entrapment of glucose oxidase (GOx) within metallic gold converts this widely used enzyme into a general saccharide oxidase. The following sugar molecules were oxidized by the entrapped enzyme (in addition to d-glucose): fructose, xylose, l-glucose, glucose-6-phosphate, sucrose, lactose, methylglucoside, and the tri-saccharide raffinose. With the exception of raffinose, none of these sugars have a natural specific oxidase. The origin of this generalization of activity is attributed to the strong protein-gold 3D interactions and to the strong interactions of the co-entrapped CTAB with both the gold, and the protein. It is proposed that these interactions induce conformational changes in the channel leading to the active site, which is located at the interface between the two units of the dimeric GOx protein. The observations are compatible with affecting the specific conformation change of pulling apart and opening this gate-keeper, rendering the active site accessible to a variety of substrates. The entrapment methodology was also found to increase the thermal stability of GOx up to 100 °C and to allow its convenient reuse, two features of practical importance.
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spelling pubmed-92260122022-06-25 Glucose oxidase converted into a general sugar-oxidase Baruch-Shpigler, Yael Avnir, David Sci Rep Article Entrapment of glucose oxidase (GOx) within metallic gold converts this widely used enzyme into a general saccharide oxidase. The following sugar molecules were oxidized by the entrapped enzyme (in addition to d-glucose): fructose, xylose, l-glucose, glucose-6-phosphate, sucrose, lactose, methylglucoside, and the tri-saccharide raffinose. With the exception of raffinose, none of these sugars have a natural specific oxidase. The origin of this generalization of activity is attributed to the strong protein-gold 3D interactions and to the strong interactions of the co-entrapped CTAB with both the gold, and the protein. It is proposed that these interactions induce conformational changes in the channel leading to the active site, which is located at the interface between the two units of the dimeric GOx protein. The observations are compatible with affecting the specific conformation change of pulling apart and opening this gate-keeper, rendering the active site accessible to a variety of substrates. The entrapment methodology was also found to increase the thermal stability of GOx up to 100 °C and to allow its convenient reuse, two features of practical importance. Nature Publishing Group UK 2022-06-23 /pmc/articles/PMC9226012/ /pubmed/35739181 http://dx.doi.org/10.1038/s41598-022-14957-6 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/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/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Baruch-Shpigler, Yael
Avnir, David
Glucose oxidase converted into a general sugar-oxidase
title Glucose oxidase converted into a general sugar-oxidase
title_full Glucose oxidase converted into a general sugar-oxidase
title_fullStr Glucose oxidase converted into a general sugar-oxidase
title_full_unstemmed Glucose oxidase converted into a general sugar-oxidase
title_short Glucose oxidase converted into a general sugar-oxidase
title_sort glucose oxidase converted into a general sugar-oxidase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9226012/
https://www.ncbi.nlm.nih.gov/pubmed/35739181
http://dx.doi.org/10.1038/s41598-022-14957-6
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