Bacteriophage-borne enzymes in carbohydrate chemistry. Part I. On the glycanase activity associated with particles of Klebsiella bacteriophage No. 11.
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.
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
D000941:Antigens; D001789:Blood Group Antigens; D009844:Oligosaccharides; D011135:Polysaccharides, Bacterial; D008094:Lithium; D000535:Aluminum; D006026:Glycoside Hydrolases