Abe J I, Takeda Y, Hizukuri S
Biochim Biophys Acta. 1982 Apr 21;703(1):26-33. doi: 10.1016/0167-4838(82)90006-1.
Glucoamylase (1,4-alpha-D-glucan glucohydrolase, EC 3.2.1.3) from Aspergillus niger was purified to be free from alpha-amylase and phosphatase (glucose 6-phosphate as substrate). The phosphatase was well separated from the glucoamylase by phosphocellulose ion-exchange chromatography. The glucoamylase action was prevented by the esterified phosphate groups of the substrate. Thus, the extensive action of the glucoamylase on potato starch exposed the 6-posphorylglucosyl residue of the starch at the non-reducing terminal and large molecular weight limit dextrins remained. The concomitant action of the phosphatase was necessary for the complete degradation of the starch.
黑曲霉的葡糖淀粉酶（1,4-α-D-葡聚糖葡糖水解酶，EC 3.2.1.3）被纯化至不含α-淀粉酶和磷酸酶（以葡萄糖6-磷酸为底物）。通过磷酸纤维素离子交换色谱法，磷酸酶与葡糖淀粉酶得到了很好的分离。底物的酯化磷酸基团可抑制葡糖淀粉酶的作用。因此，葡糖淀粉酶对马铃薯淀粉的广泛作用使淀粉在非还原末端的6-磷酸葡糖基残基暴露出来，留下了大分子量的极限糊精。磷酸酶的协同作用对于淀粉的完全降解是必需的。
