Unique transglycosylation potential of extracellular alpha-D-galactosidase from Talaromyces flavus
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F06%3A00048853" target="_blank" >RIV/61388971:_____/06:00048853 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Unique transglycosylation potential of extracellular alpha-D-galactosidase from Talaromyces flavus
Original language description
The transalycosylation potential of the extracellular alpha-D-galactosidase from the filamentous fungus Talaromyces flavus CCF 2686, chosen as the best enzyme from the screening, was investigated using a series of sterically hindered alcohols (primary, secondary and tertiary) as galactosyl acceptors. Nine alkyl alpha-D-galactopyranosides derived from the following alcohols - tert-butyl alcohol, 2-methyl-2-butyl alcohol, 2-methyl-1-propyl alcohol, 2,2,2-trifluoroethyl alcohol, 2-propyn-1-ol, n-pentyl alcohol, 3,5-dihydroxybenzyl alcohol, 1-phenylethyl alcohol and 1,4-dithio-DL-threitol - were prepared on a semi-preparative scale. This demonstrates a broad synthetic potential of the T flavus alpha-D-galactosidase that has not been observed with another enzyme tested. Moreover, this enzyme exhibits good transglycosylation yields (6-34%). The enzymatic synthesis of tert-butyl alpha-D-galactopyranoside by transglycosylation was studied in detail
Czech name
Jedinečný transglycosylační potenciál extracelulární alpha-D-galactosidasy z Talaromyces flavus
Czech description
Byl studován transglykosylační potenciál extracelulární alpha-D-galactosidasy z Talaromyces flavus s použitím serie stericky bráněných alkoholů
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EE - Microbiology, virology
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2006
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Molecular Catalysis B-Enzymatic
ISSN
1381-1177
e-ISSN
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Volume of the periodical
39
Issue of the periodical within the volume
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Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
7
Pages from-to
128-134
UT code for WoS article
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EID of the result in the Scopus database
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