吸水链霉菌海藻糖酶的部分纯化及性质
Partial prufication and properties of a trehalase from Streptomyces hygroscopicus.
作者信息
Hey A E, Elbein A D
出版信息
J Bacteriol. 1968 Jul;96(1):105-10. doi: 10.1128/jb.96.1.105-110.1968.
Abstract
The enzyme alpha,alpha'-glucoside 1-glucohydrolase, which catalyzes the hydrolysis of trehalose, was isolated from Streptomyces hygroscopicus and was purified approximately 80-fold. The enzyme was completely specific for trehalose as substrate. None of the other naturally occurring glucose disaccharides exhibited any significant activity. The pH optimum for enzymatic activity was found to be 6.5 and the K(m) was estimated to be approximately 1.8 x 10(-2)m. The product of the reaction was identified as d-glucose by chemical, chromatographic, and enzymatic methods. The presence of this enzyme was demonstrated in several species of Streptomyces and related organisms.
摘要
从吸水链霉菌中分离出催化海藻糖水解的α,α'-葡糖苷1-葡糖水解酶，并将其纯化了约80倍。该酶对海藻糖作为底物具有完全特异性。其他天然存在的葡萄糖二糖均未表现出任何显著活性。发现酶活性的最适pH为6.5，米氏常数（K(m)）估计约为1.8×10⁻²m。通过化学、色谱和酶学方法将反应产物鉴定为d-葡萄糖。在几种链霉菌属和相关生物体中证实了这种酶的存在。
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