Saadat S, Kamisango K, Ballou C E, Dell A
Carbohydr Res. 1986 May 1;148(2):309-19. doi: 10.1016/s0008-6215(00)90398-7.
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.
在米根霉霉菌中检测到一种催化α-(1→4)-连接的6-O-甲基-D-葡聚糖水解的酶活性，并从该霉菌中进行了纯化。该酶的作用类似于α淀粉酶，消化未修饰的淀粉寡糖的速度是其消化6-O-甲基和6-脱氧衍生物速度的10至15倍。用胰α淀粉酶和曲霉葡糖淀粉酶消化分枝杆菌O-甲基-D-葡萄糖多糖得到的极限产物，再用根霉α淀粉酶进一步消化时，会释放出由α-(1→4)-连接的6-O-甲基-D-葡萄糖组成的二糖、三糖和四糖片段。分子的其余部分以由两个或三个α-(1→4)-连接的6-O-甲基-D-葡萄糖残基终止的寡糖形式回收。
