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Glycosidases: a key to tailored carbohydrates

Paper ID Volume ID Publish Year Pages File Format Full-Text
37660 45381 2009 11 PDF Available
Title
Glycosidases: a key to tailored carbohydrates
Abstract

In recent years, carbohydrate-processing enzymes have become the enzymes of choice in many applications thanks to their stereoselectivity and efficiency. This review presents recent developments in glycosidase-catalyzed synthesis via two complementary approaches: the use of wild-type enzymes with engineered substrates, and mutant glycosidases. Genetic engineering has recently produced glucuronyl synthases, an inverting xylosynthase and the first mutant endo-β-N-acetylglucosaminidase. A thorough selection of enzyme strains and aptly modified substrates have resulted in rare glycostructures, such as N-acetyl-β-galactosaminuronates, β1,4-linked mannosides and α1,4-linked galactosides. The efficient selection of mutant enzymes is facilitated by high-throughput screening assays involving the co-expression of coupled enzymes or chemical complementation. Selective glycosidase inhibitors and highly specific glycosidases are finding attractive applications in biomedicine, biology and proteomics.

First Page Preview
Glycosidases: a key to tailored carbohydrates
Publisher
Database: Elsevier - ScienceDirect
Journal: - Volume 27, Issue 4, April 2009, Pages 199–209
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering