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dc.contributor.authorBulmer, Gregory S; orcid: 0000-0003-4794-2858
dc.contributor.authorMattey, Ashley P; orcid: 0000-0002-6564-7150
dc.contributor.authorParmeggiani, Fabio
dc.contributor.authorWilliams, Ryan
dc.contributor.authorLedru, Helene
dc.contributor.authorMarchesi, Andrea; orcid: 0000-0002-1560-5921
dc.contributor.authorSeibt, Lisa S; orcid: 0000-0002-8230-5371
dc.contributor.authorBoth, Peter
dc.contributor.authorHuang, Kun
dc.contributor.authorGalan, M Carmen; orcid: 0000-0001-7307-2871
dc.contributor.authorFlitsch, Sabine L; orcid: 0000-0003-3974-646X
dc.contributor.authorGreen, Anthony P; orcid: 0000-0003-0454-1798
dc.contributor.authorvan Munster, Jolanda M; orcid: 0000-0003-0412-7001
dc.date.accessioned2021-06-23T00:33:32Z
dc.date.available2021-06-23T00:33:32Z
dc.date.issued2021-06-08
dc.identifierpubmed: 34105582
dc.identifierdoi: 10.1039/d1ob00971k
dc.identifier.citationOrganic & biomolecular chemistry
dc.identifier.urihttp://hdl.handle.net/10034/625019
dc.descriptionFrom PubMed via Jisc Publications Router
dc.descriptionPublication status: aheadofprint
dc.description.abstractPromiscuous 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.
dc.languageeng
dc.sourceeissn: 1477-0539
dc.titleA promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes.
dc.typearticle
dc.date.updated2021-06-23T00:33:32Z


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