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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.
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