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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| Format: | Article |
| Language: | English |
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Nature Portfolio
2021-05-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-021-90242-2 |
| _version_ | 1818424798275960832 |
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| author | Yael Baruch-Shpigler David Avnir |
| author_facet | Yael Baruch-Shpigler David Avnir |
| author_sort | Yael Baruch-Shpigler |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-14T14:03:46Z |
| format | Article |
| id | doaj.art-06935cdd2ba74a03a8f9d1e09ef4ae70 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-14T14:03:46Z |
| publishDate | 2021-05-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-06935cdd2ba74a03a8f9d1e09ef4ae702022-12-21T22:58:38ZengNature PortfolioScientific Reports2045-23222021-05-0111111010.1038/s41598-021-90242-2Entrapment of glucose oxidase within gold converts it to a general monosaccharide-oxidaseYael Baruch-Shpigler0David Avnir1Institute of Chemistry and the Center for Nanoscience and Nanotechnology, The Hebrew University of JerusalemInstitute of Chemistry and the Center for Nanoscience and Nanotechnology, The Hebrew University of JerusalemAbstract 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.https://doi.org/10.1038/s41598-021-90242-2 |
| spellingShingle | Yael Baruch-Shpigler David Avnir Entrapment of glucose oxidase within gold converts it to a general monosaccharide-oxidase Scientific Reports |
| title | 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_short | 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 |
| url | https://doi.org/10.1038/s41598-021-90242-2 |
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