Entrapment of glucose oxidase within gold converts it to a general monosaccharide-oxidase

Abstract We report that entrapping glucose oxidase (GOx) within metallic gold, expands its activity to become an oxidase for monosaccharides that do not have a natural enzyme with that activity—fructose and xylose—and that this entrapment also removes the enantioselectivity, rendering this enzyme ca...

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Autores principales:	Yael Baruch-Shpigler, David Avnir
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/06935cdd2ba74a03a8f9d1e09ef4ae70
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spelling	oai:doaj.org-article:06935cdd2ba74a03a8f9d1e09ef4ae702021-12-02T15:49:40ZEntrapment of glucose oxidase within gold converts it to a general monosaccharide-oxidase10.1038/s41598-021-90242-22045-2322https://doaj.org/article/06935cdd2ba74a03a8f9d1e09ef4ae702021-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-90242-2https://doaj.org/toc/2045-2322Abstract We report that entrapping glucose oxidase (GOx) within metallic gold, expands its activity to become an oxidase for monosaccharides that do not have a natural enzyme with that activity—fructose and xylose—and that this entrapment also removes the enantioselectivity, rendering this enzyme capable of oxidizing the “wrong” l-enantiomer of glucose. These observations suggest that in this biomaterial adsorptive interactions of the outer regions of the protein with the gold cage, pull apart and widen the tunnel between the two monomeric units of GOx, to a degree that its stereoselectivity is compromised; then, the active sites which are more versatile than currently attributed to, are free and capable of acting on the foreign sugars. To test this proposition, we entrapped in gold l-asparaginase, which is also a dimeric enzyme (a dimer of tight dimers), and found, again, that this metallic biomaterial widens the activity of that enzyme, to include the D-amino acid counter enantiomer as well. Detailed kinetic analyses for all substrates are provided for the gold bio-composites, including determination of the difference between the activation energies towards two opposite enantiomers.Yael Baruch-ShpiglerDavid AvnirNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yael Baruch-Shpigler David Avnir Entrapment of glucose oxidase within gold converts it to a general monosaccharide-oxidase
description	Abstract We report that entrapping glucose oxidase (GOx) within metallic gold, expands its activity to become an oxidase for monosaccharides that do not have a natural enzyme with that activity—fructose and xylose—and that this entrapment also removes the enantioselectivity, rendering this enzyme capable of oxidizing the “wrong” l-enantiomer of glucose. These observations suggest that in this biomaterial adsorptive interactions of the outer regions of the protein with the gold cage, pull apart and widen the tunnel between the two monomeric units of GOx, to a degree that its stereoselectivity is compromised; then, the active sites which are more versatile than currently attributed to, are free and capable of acting on the foreign sugars. To test this proposition, we entrapped in gold l-asparaginase, which is also a dimeric enzyme (a dimer of tight dimers), and found, again, that this metallic biomaterial widens the activity of that enzyme, to include the D-amino acid counter enantiomer as well. Detailed kinetic analyses for all substrates are provided for the gold bio-composites, including determination of the difference between the activation energies towards two opposite enantiomers.
format	article
author	Yael Baruch-Shpigler David Avnir
author_facet	Yael Baruch-Shpigler David Avnir
author_sort	Yael Baruch-Shpigler
title	Entrapment of glucose oxidase within gold converts it to a general monosaccharide-oxidase
title_short	Entrapment of glucose oxidase within gold converts it to a general monosaccharide-oxidase
title_full	Entrapment of glucose oxidase within gold converts it to a general monosaccharide-oxidase
title_fullStr	Entrapment of glucose oxidase within gold converts it to a general monosaccharide-oxidase
title_full_unstemmed	Entrapment of glucose oxidase within gold converts it to a general monosaccharide-oxidase
title_sort	entrapment of glucose oxidase within gold converts it to a general monosaccharide-oxidase
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/06935cdd2ba74a03a8f9d1e09ef4ae70
work_keys_str_mv	AT yaelbaruchshpigler entrapmentofglucoseoxidasewithingoldconvertsittoageneralmonosaccharideoxidase AT davidavnir entrapmentofglucoseoxidasewithingoldconvertsittoageneralmonosaccharideoxidase
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Entrapment of glucose oxidase within gold converts it to a general monosaccharide-oxidase

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