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Vester-Christensen, Malene Bech, Holck, Jesper, Rejzek, Martin, Perrin, Léa, Tovborg, Morten, Svensson, Birte, Field, Robert A. 
ORCID: https://orcid.org/0000-0001-8574-0275 and Møller, Marie Sofie
(2023)
Exploration of the transglycosylation activity of barley limit dextrinase for production of novel glycoconjugates.
Molecules, 28 (10).
ISSN 1420-3049
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Abstract
A few α-glucan debranching enzymes (DBEs) of the large glycoside hydrolase family 13 (GH13), also known as the α-amylase family, have been shown to catalyze transglycosylation as well as hydrolysis. However, little is known about their acceptor and donor preferences. Here, a DBE from barley, limit dextrinase (HvLD), is used as a case study. Its transglycosylation activity is studied using two approaches; (i) natural substrates as donors and different p-nitrophenyl (pNP) sugars as well as different small glycosides as acceptors, and (ii) α-maltosyl and α-maltotriosyl fluorides as donors with linear maltooligosaccharides, cyclodextrins, and GH inhibitors as acceptors. HvLD showed a clear preference for pNP maltoside both as acceptor/donor and acceptor with the natural substrate pullulan or a pullulan fragment as donor. Maltose was the best acceptor with α-maltosyl fluoride as donor. The findings highlight the importance of the subsite +2 of HvLD for activity and selectivity when maltooligosaccharides function as acceptors. However, remarkably, HvLD is not very selective when it comes to aglycone moiety; different aromatic ring-containing molecules besides pNP could function as acceptors. The transglycosylation activity of HvLD can provide glycoconjugate compounds with novel glycosylation patterns from natural donors such as pullulan, although the reaction would benefit from optimization.
| Item Type: | Article |
|---|---|
| Additional Information: | Data Availability Statement: The data presented in this study are available on request from the corresponding author. Funding Information: This research was funded by the Novo Nordisk Foundation, grant number NNF19OC0055482, to M.S.M. The work was supported by a Ph.D. scholarship from Technical University of Denmark to M.B.V.-C. We thank the John Innes Centre for supporting elements of this work. |
| Uncontrolled Keywords: | cazyme profiling,cyclodextrins,glycoside hydrolase family 13,glycosyl fluorides,pullulan,α-glucan debranching enzyme,analytical chemistry,chemistry (miscellaneous),molecular medicine,pharmaceutical science,drug discovery,physical and theoretical chemistry,organic chemistry ,/dk/atira/pure/subjectarea/asjc/1600/1602 |
| Faculty \ School: | Faculty of Science > School of Chemistry, Pharmacy and Pharmacology |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 03 Sep 2024 15:35 |
| Last Modified: | 25 Sep 2024 18:04 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/96479 |
| DOI: | 10.3390/molecules28104111 |
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