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J Bacteriol. 1968 July; 96(1): 105-110
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

Partial Purification and Properties of a Trehalase from Streptomyces hygroscopicus

^a Department of Biology, Rice University, Houston, Texas 77001

ABSTRACT

The enzyme ,'-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^–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.

¹ Recipient of a Research Career Development Award from the National Institute of Allergy and Infectious Diseases.