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Titolo:
APPLICATION OF A CHEMOENZYMATIC GLYCOSYLATION METHOD TO ALPHA-CHYMOTRYPSIN AND CANDIDA-RUGOSA LIPASE SURFACE MODIFICATIONS
Autore:
LONGO MA; COMBES D;
Indirizzi:
INST NATL SCI APPL,CTR BIOINGN GILBERT DURAND,URA CNRS 544,COMPLEXE SCI RANGUEIL F-31077 TOULOUSE FRANCE INST NATL SCI APPL,CTR BIOINGN GILBERT DURAND,URA CNRS 544 F-31077 TOULOUSE FRANCE
Titolo Testata:
Journal of molecular catalysis. B, Enzymatic
fascicolo: 6, volume: 2, anno: 1997,
pagine: 281 - 289
SICI:
1381-1177(1997)2:6<281:AOACGM>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
SOLUBLE POLYSACCHARIDES; THERMAL STABILIZATION; PROTEIN STABILIZATION; COVALENT ATTACHMENT; BETA-GALACTOSIDASE; ENZYMES; DEXTRAN; STABILITY; HYDROPHILIZATION; CASEIN;
Keywords:
ALPHA-CHYMOTRYPSIN; LIPASE; GLYCOSYLATION; HYDROPHILICITY; ACTIVITY; KINETIC CONSTANTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
M.A. Longo e D. Combes, "APPLICATION OF A CHEMOENZYMATIC GLYCOSYLATION METHOD TO ALPHA-CHYMOTRYPSIN AND CANDIDA-RUGOSA LIPASE SURFACE MODIFICATIONS", Journal of molecular catalysis. B, Enzymatic, 2(6), 1997, pp. 281-289

Abstract

A recently developed chemoenzymatic glycosylation procedure has been successfully applied on two hydrolytic enzymes, alpha-chymotrypsin andCandida rugosa lipase. First, a number of sucrose molecules have beenbound to the surface lysine residues and then, lengthening of the glycosidic chains has been carried out by the action of a levansucrase from Bacillus subtilis. For both steps, reaction conditions have been studied in order to obtain a range of glycosylation degrees. The influence of glycoside binding on biocatalyst surface characteristics has been assessed and a progressive increase in global enzyme hydrophilic character with glycosylation has been observed. Besides, the study of hydrolytic activity and kinetic constants showed that the performed modifications brought about a certain decrease in enzyme hydrolytic activity and very slight variations in enzyme-substrate affinity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 12:02:43