alpha-L-Fucosidase from Paenibacillus thiaminolyticus: Its hydrolytic and transglycosylation abilities.
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F13%3A43896538" target="_blank" >RIV/60461373:22330/13:43896538 - isvavai.cz</a>
Alternative codes found
RIV/60461373:22810/13:43896538
Result on the web
<a href="http://dx.doi.org/10.1093/glycob/cwt041" target="_blank" >http://dx.doi.org/10.1093/glycob/cwt041</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/glycob/cwt041" target="_blank" >10.1093/glycob/cwt041</a>
Alternative languages
Result language
angličtina
Original language name
alpha-L-Fucosidase from Paenibacillus thiaminolyticus: Its hydrolytic and transglycosylation abilities.
Original language description
In this work, focused on possible application of alpha-l-fucosidases from bacterial sources in the synthesis of alpha-l-fucosylated glycoconjugates, several nonpathogenic aerobic bacterial strains were screened for alpha-l-fucosidase activity. Among themPaenibacillus thiaminolyticus was confirmed as a potent producer of enzyme with the ability to cleave the chromogenic substrate p-nitrophenyl alpha-l-fucopyranoside. The gene encoding alpha-l-fucosidase was found using the genomic library of P. thiaminolyticus constructed in the cells of Escherichia coli DH5 alpha and sequenced (EMBL database: FN869117, carbohydrate-active enzymes database: Glycosidase family 29). The enzyme was expressed in the form of polyhistidine-tagged protein (51.2 kDa) in Escherichia coli BL21 (DE3) cells, purified using nickel-nitrilotriacetic acid agarose affinity chromatography and characterized using the chromogenic substrate p-nitrophenyl alpha-l-fucopyranoside (K-m = (0.44 +/- 0.02) mmol/L, K-S = (83 +/- 8
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/LD13024" target="_blank" >LD13024: Chemoinformatics for glycosynthesis</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Glycobiology
ISSN
0959-6658
e-ISSN
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Volume of the periodical
23
Issue of the periodical within the volume
9
Country of publishing house
US - UNITED STATES
Number of pages
14
Pages from-to
1052-1065
UT code for WoS article
000322340200006
EID of the result in the Scopus database
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