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)

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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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