Beta-1,3-galactosyl-N-acetylhexosamine phosphorylase from Bifidobacterium bifidum DSM 20082: characterization, partial purification and relation to mucin degradation

Autor:	D, Derensy-Dron, F, Krzewinski, C, Brassart, S, Bouquelet
Rok vydání:	1999
Předmět:	Swine Galactosephosphates Molecular Sequence Data Mucins Temperature Hydrogen-Ion Concentration Disaccharides Galactosyltransferases Substrate Specificity Bacterial Proteins Carbohydrate Sequence Carbohydrate Conformation Animals Bifidobacterium Phosphorylation
Zdroj:	Biotechnology and applied biochemistry. 29
ISSN:	0885-4513
Popis:	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 Pi, the phosphorolysis reaction was favoured and was accompanied by a Walden reaction. Cleavage of the beta-glycosidic linkage gave an alpha-galactoside derivative (alpha-D-galactose 1-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.-.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::3a62c65207796b58c4c9aacee83ab500 https://pubmed.ncbi.nlm.nih.gov/9889079 Zobrazit plný text záznamu Plný text