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Titolo:
beta-1,3-Galactosyl-N-acetylhexosamine phosphorylase from Bifidobacterium bifidum DSM 20082: characterization, partial purification and relation to mucin degradation
Autore:
Derensy-Dron, D; Krzewinski, F; Brassart, C; Bouquelet, S;
Indirizzi:
Univ Sci & Tech Lille Flandres Artois, UMR 111 CNRS, Chim Biol Lab, F-59655 Univ Sci & Tech Lille Flandres Artois Villeneuve Dascq France F-59655 55
Titolo Testata:
BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
, volume: 29, anno: 1999,
parte:, 1
pagine: 3 - 10
SICI:
0885-4513(199902)29:<3:BPFBB>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
GAS-LIQUID-CHROMATOGRAPHY; METHYL GLYCOSIDES; TREHALOSE PHOSPHORYLASE; MASS-SPECTROMETRY; ESCHERICHIA-COLI; GLYCOPROTEINS; BACTERIA; INFANTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Bouquelet, S Univ Sci & Tech Lille Flandres Artois, UMR 111 CNRS, Chim Biol Lab, F-59655 Univ Sci & Tech Lille Flandres Artois Villeneuve Dascq France F-59655
Citazione:
D. Derensy-Dron et al., "beta-1,3-Galactosyl-N-acetylhexosamine phosphorylase from Bifidobacterium bifidum DSM 20082: characterization, partial purification and relation to mucin degradation", BIOT APP B, 29, 1999, pp. 3-10

Abstract

A new enzyme has been characterized in a cell-free extract of Bifidobacterium bifidum that catalysed the reversible phosphorolytic cleavage of beta-1,3-galacto-oligosaccharides. In the presence of P-i, the phosphorolysis reaction was favoured and was accompanied by a Warden reaction. cleavage of the beta-glycosidic linkage gave an alpha-galactoside derivative (alpha-D-galactose I-phosphate). The enzyme possesses a high specificity for beta-D-galactosido-(1,3)-N-acetylglucosamine and beta-D-galactosido-(1,3)-N-acetylgalactosamine. This purified intracellular enzyme had an estimated molecular mass of 140 kDa. The galactophosphorolytic activity on disaccharides was optimal at: pH 6-6.5 and the reverse reaction was optimal at pH 5.5-6, The temperature optimum for phosphorolysis and the reverse reaction was approx. 50-55 degrees C. This enzyme is of particular interest in degrading some beta-D-Gal(1,3) linkages and should be classified as EC 2.4.1.-.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 18:53:23