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Titolo: A NOVEL CHEMOENZYMATIC GLYCOSYLATION STRATEGY - APPLICATION TO LYSOZYME MODIFICATION
Autore: LONGO MA; COMBES D;
- Indirizzi:
- INST NATL SCI APPL,CTR BIOINGN GILBERT DURAND,CNRS,URA 544,COMPLEXE SCI RANGUEIL F-31077 TOULOUSE FRANCE INST NATL SCI APPL,CTR BIOINGN GILBERT DURAND,CNRS,URA 544 F-31077 TOULOUSE FRANCE
- Titolo Testata:
- FEBS letters
fascicolo: 1-2,
volume: 375,
anno: 1995,
pagine: 63 - 66
- SICI:
- 0014-5793(1995)375:1-2<63:ANCGS->2.0.ZU;2-G
- Fonte:
- ISI
- Lingua:
- ENG
- Soggetto:
- SOLUBLE POLYSACCHARIDES; THERMAL STABILIZATION; COVALENT ATTACHMENT; BETA-GALACTOSIDASE; ALPHA-CHYMOTRYPSIN; ENZYMES; STABILITY; PROTEINS; DEXTRAN;
- Keywords:
- GLYCOSYLATION; LYSOZYME; GLYCOSYLTRANSFERASE; HYDROPHOBICITY; STABILITY;
- Tipo documento:
- Article
- Natura:
- Periodico
- Settore Disciplinare:
- Science Citation Index Expanded
- Science Citation Index Expanded
- Citazioni:
- 23
- Recensione:
- Indirizzi per estratti:
-
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- Citazione:
- M.A. Longo e D. Combes, "A NOVEL CHEMOENZYMATIC GLYCOSYLATION STRATEGY - APPLICATION TO LYSOZYME MODIFICATION", FEBS letters, 375(1-2), 1995, pp. 63-66
Abstract
Hen egg lysozyme has been non-specifically glycosylated using a noveltwo-step strategy, First, a number of sucrose molecules have been chemically bound to the protein surface lysines, then the glycosidic chains have been enzymically lengthened, using a glycosyltransferase. For this task, a fructosyltransferase and a levansucrase have been tested,the latter appearing as the most effective one, In all cases, reactions have been optimised and several degrees of modification have been obtained, Finally, the effects of the modifications on lysozyme hydrophobicity, hydrolytic activity, hydrolysis substrate affinity and thermostability have been assessed.
ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 19:59:48