Enzymic degradation of the mycobacterial O-methyl-D-glucose polysaccharide by a Rhizopus-mold alpha amylase, an enzyme active on 6-O-methyl-amylo-oligosaccharides.
An enzyme activity that catalyzes hydrolysis of an alpha-(1----4)-linked 6-O-methyl-D-glucan was detected in, and purified from, Rhizopus oryzae mold. The enzyme acts like an alpha amylase and digests unmodified amylo-oligosaccharides 10 to 15 times as fast as it does the 6-O-methyl and 6-deoxy derivatives. When the limit product obtained by digesting the mycobacterial O-methyl-D-glucose polysaccharide with pancreatic alpha amylase and Aspergillus glucoamylase was further digested with the Rhizopus alpha amylase, di-, tri-, and tetra-saccharide fragments composed of alpha-(1----4)-linked 6-O-methyl-D-glucose were released. The rest of the molecule was recovered as oligosaccharides terminated by two, or three, alpha-(1----4)-linked 6-O-methyl-D-glucose residues.
D002236:Carbohydrate Conformation; D007700:Kinetics; D008745:Methylation; D009161:Mycobacterium / Q000276:immunology*; D009844:Oligosaccharides / Q000302:isolation & purification; D011135:Polysaccharides, Bacterial / Q000378:metabolism*; D012233:Rhizopus / Q000201:enzymology*; D013379:Substrate Specificity; D000516:alpha-Amylases / Q000302:isolation & purification / Q000378:metabolism*
D009844:Oligosaccharides; D011135:Polysaccharides, Bacterial; D000516:alpha-Amylases