从枯草芽孢杆菌中纯化一种新型淀粉酶及其受小麦蛋白的抑制作用
The purification of a novel amylase from Bacillus subtilis and its inhibition by wheat proteins.
作者信息
Orlando A R, Ade P, Di Maggio D, Fanelli C, Vittozzi L
出版信息
Biochem J. 1983 Feb 1;209(2):561-4. doi: 10.1042/bj2090561.
A new alpha-amylase (EC 3.2.1.1) from Bacillus subtilis was purified by affinity chromatography. The molecular weight of the purified enzyme, estimated from sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, was 93000, which is very different from the molecular weights of two well-characterized amylases from B. subtilis. Electrofocusing showed an isoelectric point of 5. Amylase shows a broad maximum of activity between pH 6 and 7; maximal inhibition of enzyme by wheat-protein alpha-amylase inhibitors is displayed at pH 7.
通过亲和色谱法从枯草芽孢杆菌中纯化出一种新型α-淀粉酶（EC 3.2.1.1）。根据十二烷基硫酸钠/聚丙烯酰胺凝胶电泳估算，纯化酶的分子量为93000，这与枯草芽孢杆菌中两种已充分表征的淀粉酶的分子量有很大差异。等电聚焦显示其等电点为5。淀粉酶在pH 6至7之间表现出广泛的活性最大值；小麦蛋白α-淀粉酶抑制剂对该酶的最大抑制作用在pH 7时表现出来。
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