Enzymatic synthesis of N-acetyllactosamine from lactose enabled by recombinant β1,4-galactosyltransferases.

Abstract

Utilising a fast and sensitive screening method based on imidazolium-tagged probes, we report unprecedented reversible activity of bacterial β1,4-galactosyltransferases to catalyse the transgalactosylation from lactose to N-acetylglucosamine to form N-acetyllactosamine in the presence of UDP. The process is demonstrated by the preparative scale synthesis of pNP-β-LacNAc from lactose using β1,4-galactosyltransferase NmLgtB-B as the only biocatalyst.

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Item Type:	Article
Authors/Creators:	Huang, K Parmeggiani, F Ledru, H Hollingsworth, K Mas Pons, J Marchesi, A Both, P Mattey, AP Pallister, E Bulmer, GS van Munster, JM Turnbull, WB https://orcid.org/0000-0002-7352-0360 Galan, MC Flitsch, SL
Copyright, Publisher and Additional Information:	© The Royal Society of Chemistry 2019. This is an author produced version of a paper published in Organic and Biomolecular Chemistry. Uploaded in accordance with the publisher's self-archiving policy.
Dates:	Published: 28 June 2019 Published (online): 30 May 2019 Accepted: 29 May 2019
Institution:	The University of Leeds
Academic Units:	The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) > Organic Chemistry (Leeds)
Depositing User:	Symplectic Publications
Date Deposited:	28 Jun 2019 11:07
Last Modified:	30 May 2020 00:38
Status:	Published
Publisher:	Royal Society of Chemistry
Identification Number:	10.1039/C9OB01089K
Related URLs:	PubMed URL
Open Archives Initiative ID (OAI ID):	oai:eprints.whiterose.ac.uk:147918

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Enzymatic synthesis of N-acetyllactosamine from lactose enabled by recombinant β1,4-galactosyltransferases.

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