Purification and properties of thermostable xylanase and beta-xylosidase produced by a newly isolated Bacillus stearothermophilus strain

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Purification and characterization of an acidic, thermophilic phytase from a newly isolated Geobacillus stearothermophilus strain DM12

Microbial phytases were applied mainly to animal and human foodstuffs in order to improvemineral bioavailability and food processing. In addition, phytases have potentialbiotechnological application in various other fields, such as environmental protection,aquaculture and agriculture. Bacillus sp. DM12, an isolate from a hot spring, produces phytase,which catalyzes the hydrolysis of phytic acid...

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Purification and Some Properties of a Thermostable Protease, BSP2, Produced from Bacillus stearothermophilus No. 2

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Overexpression and single-step purification of a thermostable xylanase from Bacillus stearothermophilus T-6.

Xylanase T-6 is a thermostable alkaline-tolerant enzyme that is produced by Bacillus stearothermophilus T-6. Xylanase T-6 was found to bleach pulp effectively at pH 9 and 65 degrees C and was used successfully on an industrial-scale mill trial. To facilitate the future characterization of the protein via X-ray analysis and protein engineering, it was necessary to overexpress the enzyme in Esche...

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Isolation and Partial Characterization of a Bacterial Thermostable Polymethyl Galacturonase from a Newly Isolated Bacillus sp. strain BR1390

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purification and characterization of an acidic, thermophilic phytase from a newly isolated geobacillus stearothermophilus strain dm12

microbial phytases were applied mainly to animal and human foodstuffs in order to improvemineral bioavailability and food processing. in addition, phytases have potentialbiotechnological application in various other fields, such as environmental protection,aquaculture and agriculture. bacillus sp. dm12, an isolate from a hot spring, produces phytase,which catalyzes the hydrolysis of phytic acid...

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ژورنال

عنوان ژورنال: Journal of Bacteriology

سال: 1990

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.172.12.6669-6672.1990