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A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes
Promiscuous activity of a glycosyltransferase was exploited to polymerise glucose from UDP-glucose via the generation of β-1,4-glycosidic linkages. The biocatalyst was incorporated into biocatalytic cascades and chemo-enzymatic strategies to synthesise cello-oligosaccharides with tailored functional...
| Autores principales: | , , , , , , , , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
The Royal Society of Chemistry
2021
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8243248/ https://www.ncbi.nlm.nih.gov/pubmed/34105582 http://dx.doi.org/10.1039/d1ob00971k |
| _version_ | 1783715722663297024 |
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| author | Bulmer, Gregory S. Mattey, Ashley P. Parmeggiani, Fabio Williams, Ryan Ledru, Helene Marchesi, Andrea Seibt, Lisa S. Both, Peter Huang, Kun Galan, M. Carmen Flitsch, Sabine L. Green, Anthony P. van Munster, Jolanda M. |
| author_facet | Bulmer, Gregory S. Mattey, Ashley P. Parmeggiani, Fabio Williams, Ryan Ledru, Helene Marchesi, Andrea Seibt, Lisa S. Both, Peter Huang, Kun Galan, M. Carmen Flitsch, Sabine L. Green, Anthony P. van Munster, Jolanda M. |
| author_sort | Bulmer, Gregory S. |
| collection | PubMed |
| description | Promiscuous activity of a glycosyltransferase was exploited to polymerise glucose from UDP-glucose via the generation of β-1,4-glycosidic linkages. The biocatalyst was incorporated into biocatalytic cascades and chemo-enzymatic strategies to synthesise cello-oligosaccharides with tailored functionalities on a scale suitable for employment in mass spectrometry-based assays. The resulting glycan structures enabled reporting of the activity and selectivity of celluloltic enzymes. |
| format | Online Article Text |
| id | pubmed-8243248 |
| institution | National Center for Biotechnology Information |
| language | English |
| publishDate | 2021 |
| publisher | The Royal Society of Chemistry |
| record_format | MEDLINE/PubMed |
| spelling | pubmed-82432482021-07-12 A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes Bulmer, Gregory S. Mattey, Ashley P. Parmeggiani, Fabio Williams, Ryan Ledru, Helene Marchesi, Andrea Seibt, Lisa S. Both, Peter Huang, Kun Galan, M. Carmen Flitsch, Sabine L. Green, Anthony P. van Munster, Jolanda M. Org Biomol Chem Chemistry Promiscuous activity of a glycosyltransferase was exploited to polymerise glucose from UDP-glucose via the generation of β-1,4-glycosidic linkages. The biocatalyst was incorporated into biocatalytic cascades and chemo-enzymatic strategies to synthesise cello-oligosaccharides with tailored functionalities on a scale suitable for employment in mass spectrometry-based assays. The resulting glycan structures enabled reporting of the activity and selectivity of celluloltic enzymes. The Royal Society of Chemistry 2021-06-01 /pmc/articles/PMC8243248/ /pubmed/34105582 http://dx.doi.org/10.1039/d1ob00971k Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/ |
| spellingShingle | Chemistry Bulmer, Gregory S. Mattey, Ashley P. Parmeggiani, Fabio Williams, Ryan Ledru, Helene Marchesi, Andrea Seibt, Lisa S. Both, Peter Huang, Kun Galan, M. Carmen Flitsch, Sabine L. Green, Anthony P. van Munster, Jolanda M. A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes |
| title | A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes |
| title_full | A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes |
| title_fullStr | A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes |
| title_full_unstemmed | A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes |
| title_short | A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes |
| title_sort | promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes |
| topic | Chemistry |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8243248/ https://www.ncbi.nlm.nih.gov/pubmed/34105582 http://dx.doi.org/10.1039/d1ob00971k |
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