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

Gregory  S Bulmer; Ashley Philip Mattey; Fabio Parmeggiani; Ryan Williams; Helene Ledru; Andrea Marchesi; Lisa Seibt; Peter Both; Kun Huang; M. Carmen Galan; Sabine L. Flitsch; Anthony Green; Jolanda Van Van Munster

doi:10.1039/D1OB00971K

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

Gregory S Bulmer, Ashley Philip Mattey, Fabio Parmeggiani, Ryan Williams, Helene Ledru, Andrea Marchesi, Lisa Seibt, Peter Both, Kun Huang, M. Carmen Galan, Sabine L. Flitsch, Anthony Green, Jolanda Van Van Munster

University of Bristol

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Journal	Organic & biomolecular chemistry
DOIs	https://doi.org/10.1039/D1OB00971K
Publication status	Published - 1 Jun 2021

Access to Document

10.1039/D1OB00971KLicence: CC BY

http://pubs.rsc.org/en/Content/ArticleLanding/2021/OB/D1OB00971K

Cite this

Bulmer, G. S., Mattey, A. P., Parmeggiani, F., Williams, R., Ledru, H., Marchesi, A., Seibt, L., Both, P., Huang, K., Galan, M. C., Flitsch, S. L., Green, A., & Van Munster, J. V. (2021). A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes. Organic & biomolecular chemistry. https://doi.org/10.1039/D1OB00971K

@article{22a48e9dad3e4e07a563318840f60588,

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

abstract = "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.",

author = "Bulmer, {Gregory S} and Mattey, {Ashley Philip} and Fabio Parmeggiani and Ryan Williams and Helene Ledru and Andrea Marchesi and Lisa Seibt and Peter Both and Kun Huang and Galan, {M. Carmen} and Flitsch, {Sabine L.} and Anthony Green and {Van Munster}, {Jolanda Van}",

year = "2021",

month = jun,

day = "1",

doi = "10.1039/D1OB00971K",

language = "English",

journal = "Organic & biomolecular chemistry",

issn = "1477-0520",

publisher = "Royal Society of Chemistry",

}

Bulmer, GS, Mattey, AP, Parmeggiani, F, Williams, R, Ledru, H, Marchesi, A, Seibt, L, Both, P, Huang, K, Galan, MC, Flitsch, SL , Green, A & Van Munster, JV 2021, 'A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes', Organic & biomolecular chemistry. https://doi.org/10.1039/D1OB00971K

TY - JOUR

T1 - A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes

AU - Bulmer, Gregory S

AU - Mattey, Ashley Philip

AU - Parmeggiani, Fabio

AU - Williams, Ryan

AU - Ledru, Helene

AU - Marchesi, Andrea

AU - Seibt, Lisa

AU - Both, Peter

AU - Huang, Kun

AU - Galan, M. Carmen

AU - Flitsch, Sabine L.

AU - Green, Anthony

AU - Van Munster, Jolanda Van

PY - 2021/6/1

Y1 - 2021/6/1

N2 - 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.

AB - 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.

U2 - 10.1039/D1OB00971K

DO - 10.1039/D1OB00971K

M3 - Article

SN - 1477-0520

JO - Organic & biomolecular chemistry

JF - Organic & biomolecular chemistry

ER -

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

Abstract

Access to Document

Fingerprint

Cite this