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

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

^*Corresponding author for this work

Head Of R&D

Research output: Contribution to journal › Short communication › peer-review

8 Citations (Scopus)

61 Downloads (Pure)

Abstract

Promiscuous activity of a glycosyltransferase was exploited to polymerise glucose from UDP-glucoseviathe 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
Pages (from-to)	5529-5533
Number of pages	5
Journal	Organic and Biomolecular Chemistry
Volume	19
Issue number	25
Early online date	1 Jun 2021
DOIs	https://doi.org/10.1039/d1ob00971k
Publication status	First published - 1 Jun 2021

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10.1039/d1ob00971kLicence: CC BY

d1ob00971kFinal published version, 1.15 MBLicence: CC BY

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Bulmer, G. S., Mattey, A. P., Parmeggiani, F., Williams, R., Ledru, H., Marchesi, A., Seibt, L. S., Both, P., Huang, K., Galan, M. C., Flitsch, S. L., Green, A. P., & van Munster, J. M. (2021). A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes. Organic and Biomolecular Chemistry, 19(25), 5529-5533. Advance online publication. https://doi.org/10.1039/d1ob00971k

@article{27796d9a6ff54b5580581db44d097da7,

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-glucoseviathe 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 P.\} and Fabio Parmeggiani and Ryan Williams and Helene Ledru and Andrea Marchesi and Seibt, \{Lisa S.\} and Peter Both and Kun Huang and Galan, \{M. Carmen\} and Flitsch, \{Sabine L.\} and Green, \{Anthony P.\} and \{van Munster\}, \{Jolanda M.\}",

year = "2021",

month = jun,

day = "1",

doi = "10.1039/d1ob00971k",

language = "English",

volume = "19",

pages = "5529--5533",

journal = "Organic and Biomolecular Chemistry",

issn = "1477-0520",

publisher = "Royal Society of Chemistry",

number = "25",

}

Bulmer, GS, Mattey, AP, Parmeggiani, F, Williams, R, Ledru, H, Marchesi, A, Seibt, LS, Both, P, Huang, K, Galan, MC, Flitsch, SL, Green, AP & van Munster, JM 2021, 'A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes', Organic and Biomolecular Chemistry, vol. 19, no. 25, pp. 5529-5533. https://doi.org/10.1039/d1ob00971k

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 et al.
In: Organic and Biomolecular Chemistry, Vol. 19, No. 25, 01.06.2021, p. 5529-5533.

Research output: Contribution to journal › Short communication › peer-review

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 P.

AU - Parmeggiani, Fabio

AU - Williams, Ryan

AU - Ledru, Helene

AU - Marchesi, Andrea

AU - Seibt, Lisa S.

AU - Both, Peter

AU - Huang, Kun

AU - Galan, M. Carmen

AU - Flitsch, Sabine L.

AU - Green, Anthony P.

AU - van Munster, Jolanda M.

PY - 2021/6/1

Y1 - 2021/6/1

N2 - Promiscuous activity of a glycosyltransferase was exploited to polymerise glucose from UDP-glucoseviathe 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-glucoseviathe 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.

UR - https://www.scopus.com/pages/publications/85108880865

U2 - 10.1039/d1ob00971k

DO - 10.1039/d1ob00971k

M3 - Short communication

C2 - 34105582

AN - SCOPUS:85108880865

SN - 1477-0520

VL - 19

SP - 5529

EP - 5533

JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

IS - 25

ER -

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

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