Application of selectively acylated glycosides for the -D-galactosidase-catalysed synthesis of disaccharides

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F03%3A00008976" target="_blank" >RIV/60461373:22330/03:00008976 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22330/03:00017270

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Application of selectively acylated glycosides for the -D-galactosidase-catalysed synthesis of disaccharides

Popis výsledku v původním jazyce

The goal of our project was to acylate selectively N-acetylhexosamines using enzymes. For this aim we tested lipases (lipase PS from Burkholderia cepacia, lipase B from Candida antarctica, porcine pancreatic lipase) and protease subtilisin from Bacilluslicheniformis. Acetylation and butyrylation of GalNAc, ManNAc and p-NP-ß-GalNAc were carried out. Acylation of GalNAc with subtilisin yielded 2-acetamido-6-O-acetyl-2-deoxy-D-galactopyranose and interestingly also its furanose form, i.e. 2-acetamido-6-O-acetyl-2-deoxy-D-galactofuranose, which were obtained in a pure and stable form. Acylation of p-NP-ß-GalNAc with lipase B yielded selectively p-nitrophenyl 2-acetamido-6-O-acetyl-2-deoxy-D-galactopyranoside. Acylation of ManNAc was considerably less feasible than that of GalNAc. ManNAc could be acylated exclusively by subtilisin to afford 2-acetamido-6-O-acyl-2-deoxy-D-mannopyranose. However, butyrylation with the same enzyme (trichloroethyl butyrate as donor) proceeded further to 2-ace

Název v anglickém jazyce

Application of selectively acylated glycosides for the -D-galactosidase-catalysed synthesis of disaccharides

Popis výsledku anglicky

The goal of our project was to acylate selectively N-acetylhexosamines using enzymes. For this aim we tested lipases (lipase PS from Burkholderia cepacia, lipase B from Candida antarctica, porcine pancreatic lipase) and protease subtilisin from Bacilluslicheniformis. Acetylation and butyrylation of GalNAc, ManNAc and p-NP-ß-GalNAc were carried out. Acylation of GalNAc with subtilisin yielded 2-acetamido-6-O-acetyl-2-deoxy-D-galactopyranose and interestingly also its furanose form, i.e. 2-acetamido-6-O-acetyl-2-deoxy-D-galactofuranose, which were obtained in a pure and stable form. Acylation of p-NP-ß-GalNAc with lipase B yielded selectively p-nitrophenyl 2-acetamido-6-O-acetyl-2-deoxy-D-galactopyranoside. Acylation of ManNAc was considerably less feasible than that of GalNAc. ManNAc could be acylated exclusively by subtilisin to afford 2-acetamido-6-O-acyl-2-deoxy-D-mannopyranose. However, butyrylation with the same enzyme (trichloroethyl butyrate as donor) proceeded further to 2-ace

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F01%2F1018" target="_blank" >GA203/01/1018: Nové enzymy a metodiky pro chemoenzymatickou syntézu bioaktivních glykosidů</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2003

Kód důvěrnosti údajů

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

Název periodika

Folia Microbiol.

ISSN

0015-5632

e-ISSN

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Svazek periodika

48

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

9

Strana od-do

329-338

Kód UT WoS článku

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EID výsledku v databázi Scopus

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