Partial Purification and Properties of a Trehalase from Streptomyces hygroscopicus
- 1 July 1968
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 96 (1) , 105-110
- https://doi.org/10.1128/jb.96.1.105-110.1968
Abstract
The enzyme α,α′-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 Km was estimated to be approximately 1.8 × 10−2m. 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.This publication has 15 references indexed in Scilit:
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