Yellowlees D
Carbohydr Res. 1980 Aug 1;83(1):109-18. doi: 10.1016/s0008-6215(00)85370-7.
A limit dextrinase has been purified 2,700-fold from ungerminated pass by affinity chromatography. The enzyme hydrolyses (1 yield 6)-alpha-d-glucosidic linkages in alpha-limit dextrins containing at least one alpha-1(1 in alpha 4)-linked d-glucose residue on either side of the susceptible linkage. The limit dextrinase also hydrolyses the polysaccharides amylopectin, amylopectin beta-limit dextrin, glycogen beta-limit dextrin, and pullulan, but has no activity towards glycogen.
通过亲和色谱法从未发芽的糊粉中纯化出一种极限糊精酶，纯化倍数达2700倍。该酶可水解α-极限糊精中（1→6）-α-D-糖苷键，这些α-极限糊精在敏感键的两侧至少含有一个α-1（α-4中为1）连接的D-葡萄糖残基。极限糊精酶还可水解支链淀粉、支链淀粉β-极限糊精、糖原β-极限糊精和支链淀粉等多糖，但对糖原无活性。
