Purification and characterization of Bacillus coagulans oligo-1,6-glucosidase

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Purification, characterization, gene cloning, and sequencing of a new beta-glucosidase from Bacillus circulans subsp. alkalophilus.

An intracellular beta-glucosidase was purified from cell extracts of Bacillus circulans subsp. alkalophilus by NAD affinity and high-performance anion-exchange chromatographies. The enzyme was active against a wide range of aryl-beta-glucosides and beta-linked disaccharides. The structural gene for beta-glucosidase was cloned in Escherichia coli. The beta-glucosidase gene consisted of an open r...

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Thermophilic Bacillus coagulans

† L.W. and Y.C. contributed equally to this study. 17 * Corresponding author. 18 Mailing address: Institute of Microbiology, Chinese Academy of Sciences, Beijing 19 100101, People’s Republic of China 20 E-mail: [email protected] (B. Yu) 21 Phone/Fax: +86-10-64806132 22 AEM Accepts, published online ahead of print on 12 September 2014 Appl. Environ. Microbiol. doi:10.1128/AEM.01864-14 Copyright © 201...

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Previous investigations have revealed that Bacillus coagulans strain 43P is sensitive to the polypeptide antibiotic nisin (O'Brien et al., 1956; Campbell and Sniff, 1959; Campbell, Sniff, and O'Brien, 1959). It has also been found that nisin is effective in the control of the flat sour spoilage of tomato juice in inoculated pack studies with this strain of B. coagulans (Campbell et al., 1959). ...

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Isolation, Purification and Characterization of a Thermophilic Alkaline Protease from Bacillus subtilis BP-36

The goal of this research was to isolate and identify the thermostable alkaline protease producing bacteria among several native Iranian microorganisms. At the end of screening program, a Bacillus subtilis BP-36 strain producing thermophilic alkaline protease was isolated from a hot spring in Ardebil province. The target enzyme was purified using a one-step Aqueous two-phase systems (ATPS) prot...

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ژورنال

عنوان ژورنال: European Journal of Biochemistry

سال: 1986

ISSN: 0014-2956,1432-1033

DOI: 10.1111/j.1432-1033.1986.tb09723.x