title: Bacteriophage-borne enzymes in carbohydrate chemistry. Part I. On the glycanase activity associated with particles of Klebsiella bacteriophage No. 11.
abstract: The preparation and use of particles of Klebsiella bacteriophage No. 11 are described. A glycanase activity associated with the viruses catalyses the depolymerization of (alkali-treated) Klebsiella serotype 11 capsular polysaccharide, ultimately to a mixture of oligosaccharides consisting of one or two repeating units. Mainly glucosidic bonds are hydrolysed. The substrate specificity of the viral enzyme has been characterized by using derivatives of serotype-11 polysaccharide, as well as 81 heterologous, bacterial, capsular glycans. It is concluded that the glycanase will (at least) also depolymerize all polysaccharides containing the unsubstituted chain-trisaccharide repeating-unit of its natural substrate.
mesh_terms: D000535:Aluminum; D000941:Antigens; D001435:Bacteriophages / Q000201:enzymology*; D001789:Blood Group Antigens; D002852:Chromatography, Ion Exchange; D004355:Drug Stability; D006026:Glycoside Hydrolases / Q000032:analysis* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007709:Klebsiella / Q000201:enzymology*; D008094:Lithium; D009844:Oligosaccharides / Q000032:analysis; D011135:Polysaccharides, Bacterial; D013045:Species Specificity; D013696:Temperature; D010948:Viral Plaque Assay
chemical_list: D000941:Antigens; D001789:Blood Group Antigens; D009844:Oligosaccharides; D011135:Polysaccharides, Bacterial; D008094:Lithium; D000535:Aluminum; D006026:Glycoside Hydrolases