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Glycosidases: a key to tailored carbohydrates
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SYSNO ASEP 0327136 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Glycosidases: a key to tailored carbohydrates Author(s) Bojarová, Pavla (MBU-M) ORCID
Křen, Vladimír (MBU-M) RID, ORCIDSource Title Trends in Biotechnology. - : Elsevier - ISSN 0167-7799
Roč. 27, č. 4 (2009), s. 199-209Number of pages 11 s. Language eng - English Country GB - United Kingdom Keywords GLYCOSYLTRANSFERASE-CATALYZED SYNTHESIS ; ALPHA-L-ARABINOFURANOSIDASE ; MUTANT GLYCOSIDASES Subject RIV EE - Microbiology, Virology R&D Projects IAA400200503 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) LC06010 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GP203/09/P024 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000265136100003 DOI 10.1016/j.tibtech.2008.12.003 Annotation 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 glycosidasecatalyzed 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-b-N-acetylglucosaminidase. A thorough selection of enzyme strains and aptly modified substrates have resulted in rare glycostructures, such as N-acetyl-b-galactosaminuronates, b1,4-linked mannosides and a1,4-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 Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2010
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