Abstract
Glycoside phosphorylases catalyse the reversible synthesis of glycosidic bonds by glycosylation with concomitant release of inorganic phosphate. The equilibrium position of such reactions can render them of limited synthetic utility, unless coupled with a secondary enzymatic step where the reaction lies heavily in favour of product. This article surveys recent works on the combined use of glycan phosphorylases with other enzymes to achieve synthetically useful processes.
Keywords: Phosphorylase, disaccharide, α-glucan, cellodextrin, high-value products, biofuel.
Protein & Peptide Letters
Title:Glycan Phosphorylases in Multi-Enzyme Synthetic Processes
Volume: 24 Issue: 8
Author(s): Giulia Pergolizzi, Sakonwan Kuhaudomlarp, Eeshan Kalita and Robert A. Field*
Affiliation:
- Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH,United Kingdom
Keywords: Phosphorylase, disaccharide, α-glucan, cellodextrin, high-value products, biofuel.
Abstract: Glycoside phosphorylases catalyse the reversible synthesis of glycosidic bonds by glycosylation with concomitant release of inorganic phosphate. The equilibrium position of such reactions can render them of limited synthetic utility, unless coupled with a secondary enzymatic step where the reaction lies heavily in favour of product. This article surveys recent works on the combined use of glycan phosphorylases with other enzymes to achieve synthetically useful processes.
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Cite this article as:
Pergolizzi Giulia , Kuhaudomlarp Sakonwan , Kalita Eeshan and Field A. Robert *, Glycan Phosphorylases in Multi-Enzyme Synthetic Processes, Protein & Peptide Letters 2017; 24 (8) . https://dx.doi.org/10.2174/0929866524666170811125109
DOI https://dx.doi.org/10.2174/0929866524666170811125109 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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