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...

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Detalles Bibliográficos
Autores principales: 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.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2021
Materias:
Chemistry
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
Descripción
Sumario: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.

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