Campus Units

Chemistry

Document Type

Article

Publication Version

Published Version

Publication Date

2021

Journal or Book Title

Chemical Science

Volume

12

Issue

1

First Page

374

Last Page

383

DOI

10.1039/D0SC05338D

Abstract

Glycosidases are an important class of enzymes for performing the selective hydrolysis of glycans. Although glycans can be hydrolyzed in principle by acidic water, hydrolysis with high selectivity using nonenzymatic catalysts is an unachieved goal. Molecular imprinting in cross-linked micelles afforded water-soluble polymeric nanoparticles with a sugar-binding boroxole in the imprinted site. Post-modification installed an acidic group near the oxygen of the targeted glycosidic bond, with the acidity and distance of the acid varied systematically. The resulting synthetic glycosidase hydrolyzed oligosaccharides and polysaccharides in a highly controlled fashion simply in hot water. These catalysts not only broke down amylose with similar selectivities to those of natural enzymes, but they also could be designed to possess selectivity not available with biocatalysts. Substrate selectivity was mainly determined by the sugar residues bound within the active site, including their spatial orientations. Separation of the product was accomplished through in situ dialysis, and the catalysts left behind could be used multiple times with no signs of degradation. This work illustrates a general method to construct synthetic glycosidases from readily available building blocks via self-assembly, covalent capture, and post-modification. In addition, controlled, precise, one-step hydrolysis is an attractive way to prepare complex glycans from naturally available carbohydrate sources.

Comments

This article is published as Li, Xiaowei, and Yan Zhao. "Synthetic glycosidases for the precise hydrolysis of oligosaccharides and polysaccharides." Chemical Science 12, no. 1 (2021): 374-383. DOI: 10.1039/D0SC05338D. Posted with permission.

Creative Commons License

Creative Commons Attribution-NonCommercial 4.0 International License
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License

Copyright Owner

The Author(s)

Language

en

File Format

application/pdf

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