Beta-1,4-Galaktosyltransferasou katalyzovaná glykosylace cukerných derivátů: Modulace enzymové aktivity alfa-laktalbuminem, imobilizace a tolerance vůči rozpouštědlům

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F06%3A00048858" target="_blank" >RIV/61388971:_____/06:00048858 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Beta-1,4-Galactosyltransferase-catalyzed glycosylation of sugar derivatives: Modulation of the enzyme activity by alpha-lactalbumin, immobilization and solvent tolerance

Popis výsledku v původním jazyce

The influence of different parameters on the activity of the beta-1,4-galactosyltransferase (beta-1,4-GalT) from bovine milk has been investigated using various acceptor and donor substrates. It was found that the "specifier" protein alpha-lactalbumin (alpha-LA), which interacts with beta-1,4-GalT forming the lactose synthase (LS) complex, is not necessary when the acceptors are different glucopyranosides, and, in some cases, it can even have an inhibitory effect, like with the complex glucosides ginsenoside Rg(1) (1) and colchicoside (2). By optimization of the reaction conditions, the galactosylated and glucosylated derivatives of 2 were prepared, using UDP-Gal and UDP-Glc as sugar donors, respectively, and characterized. Moreover, beta-1,4-GalT wascovalently immobilized on Eupergit C 250 L in the absence of alpha-LA, and the synthetic performances of this immobilized biocatalyst were evaluated

Název v anglickém jazyce

Beta-1,4-Galactosyltransferase-catalyzed glycosylation of sugar derivatives: Modulation of the enzyme activity by alpha-lactalbumin, immobilization and solvent tolerance

Popis výsledku anglicky

The influence of different parameters on the activity of the beta-1,4-galactosyltransferase (beta-1,4-GalT) from bovine milk has been investigated using various acceptor and donor substrates. It was found that the "specifier" protein alpha-lactalbumin (alpha-LA), which interacts with beta-1,4-GalT forming the lactose synthase (LS) complex, is not necessary when the acceptors are different glucopyranosides, and, in some cases, it can even have an inhibitory effect, like with the complex glucosides ginsenoside Rg(1) (1) and colchicoside (2). By optimization of the reaction conditions, the galactosylated and glucosylated derivatives of 2 were prepared, using UDP-Gal and UDP-Glc as sugar donors, respectively, and characterized. Moreover, beta-1,4-GalT wascovalently immobilized on Eupergit C 250 L in the absence of alpha-LA, and the synthetic performances of this immobilized biocatalyst were evaluated

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2006

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Molecular Catalysis B-Enzymatic

ISSN

1381-1177

e-ISSN

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Svazek periodika

39

Číslo periodika v rámci svazku

-

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

7

Strana od-do

98-104

Kód UT WoS článku

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EID výsledku v databázi Scopus

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