• A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes.

      Bulmer, Gregory S; orcid: 0000-0003-4794-2858; Mattey, Ashley P; orcid: 0000-0002-6564-7150; Parmeggiani, Fabio; Williams, Ryan; Ledru, Helene; Marchesi, Andrea; orcid: 0000-0002-1560-5921; Seibt, Lisa S; orcid: 0000-0002-8230-5371; Both, Peter; Huang, Kun; Galan, M Carmen; orcid: 0000-0001-7307-2871; et al. (2021-06-08)
      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.