Kondo H, Nakatani H, Hiromi K
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Japan.
Carbohydr Res. 1990 Sep 5;204:207-13. doi: 10.1016/0008-6215(90)84036-t.
The vitro action of human and porcine pancreatic alpha-amylases on cyclomalto-oligosaccharides (cyclodextrins) was investigated both by a high-performance liquid chromatographic analysis and a quantitative analysis of the reducing power of cyclodextrin hydrolyzates. Cyclomalto-octaose (gamma-cyclodextrin) was hydrolyzed to produce mainly maltose, but cyclomalto-hexaose and -heptaose were little affected both by human and porcine alpha-amylases. Quantitative analysis of reducing power revealed that the ring-opening rate of gamma-cyclodextrin catalyzed by human pancreatic alpha-amylase was 2.8 times slower than that catalyzed by the porcine enzyme. The number of multiple attacks on gamma-cyclodextrin and its inhibitor constants for human pancreatic alpha-amylase and porcine pancreatic alpha-amylase were almost the same.
通过高效液相色谱分析和对环糊精水解产物还原能力的定量分析，研究了人和猪胰腺α-淀粉酶对环麦芽寡糖（环糊精）的体外作用。环麦芽八糖（γ-环糊精）被水解主要生成麦芽糖，但环麦芽六糖和七糖受人和猪α-淀粉酶的影响很小。还原能力的定量分析表明，人胰腺α-淀粉酶催化γ-环糊精的开环速率比猪酶催化的慢2.8倍。人胰腺α-淀粉酶和猪胰腺α-淀粉酶对γ-环糊精的多次攻击次数及其抑制常数几乎相同。
