Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain
Article Abstract:
The mechanism of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase of a Thermus strain has been investigated. To this end, a maltogenic amylase gene was cloned in Escherichia coli from the gram-negative thermophilic Thermus strain IM6501. The transglycosylation of sugar to methyl-alpha-D-glucopyranoside by forming an alpha-(1,3)-glycosidic linkage was shown for the first time.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
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Enzymatic analysis of an amylolytic enzyme from the hyperthermophilic archaeon Pyrococcus furiosus reveals its novel catalytic properties as both an alpha-amylase and a cyclodextrin-hydrolyzing enzyme
Article Abstract:
A study done on the gene corresponding to putative amylolytic enzyme of Pyrococcus furiosus is cloned and shown in Escherichia coli and the recombinant enzyme is purified with its enzymatic characteristics examined. Studies demonstrate that the putative amylolytic enzyme of Pyrococcus furiosus is a novel amylase, possessing characteristics of both cyclodextrin-hydrolyzing enzyme and alpha-amylase.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2004
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