Purification and characterization of endo-beta-galactosidase from Escherichia freundii induced by hog gastric mucin.
作者： M.N. Fukuda
DOI: 10.1016/S0021-9258(19)69543-8
关键词:
摘要: A new procedure for inducing and purifying endo-beta-galactosidase from Escherichia freundii was described. The enzyme found to be induced with high efficiency in culture medium containing Smith-degraded hog gastric mucin, which prepared a commercially available starting material. Endo-beta-galactosidase then purified by ammonium sulfate fractionation, DEAE-Sephadex chromatography, affinity chromatography on Sepharose conjugated the mucin. thus only three steps showed no other glycosidase or protease activities had higher specific activity compared previous method. This method has great advantage since mucin is abundantly of production without significant induction exoglycosidase. hydrolysis oligosaccharides, glycosphingolipid, keratansulfate studied using this newly enzyme. Kinetic data indicate that hydrolyzability these substrates largely affected substrate concentration, concentration structure substrates. Based results, specificity E. discussed.
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