A thermostable α-amylase producing maltohexaose from a new isolated Bacillus sp. US100: study of activity and molecular cloning of the corresponding gene

A Bacillus sp. US100 strain was isolated from Tunisian hot spring soil. This strain secretes a thermoactive amylase having an optimal temperature of 82°C and a remarkable thermostability with a half time of 40 min at 110°C in the presence of 20% (w/v) of substrate. The main end products of its actio...

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Bibliographic Details
Published in:Enzyme and microbial technology 1999-06, Vol.24 (8-9), p.584-589
Main Authors: Ali, Mamdouh Ben, Mezghani, Monia, Bejar, Samir
Format: Article
Language:English
Subjects:
B. stearothermophilus
Bacillus
Bacteria
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
Catalyst activity
Enzyme kinetics
Enzymes
Fundamental and applied biological sciences. Psychology
Hydrolysis
maltohexaose
maltopentaose
Miscellaneous
Mission oriented research
molecular cloning
Molecular dynamics
Temperature
thermoamylase
Thermodynamic stability
Tunisia
α-amylase
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Summary:A Bacillus sp. US100 strain was isolated from Tunisian hot spring soil. This strain secretes a thermoactive amylase having an optimal temperature of 82°C and a remarkable thermostability with a half time of 40 min at 110°C in the presence of 20% (w/v) of substrate. The main end products of its action on starch are maltohexaose and maltopentaose which is the smallest substrate hydrolysed by this enzyme. The molecular cloning, in E. coli, of a 3-kb DNA fragment encoding for this activity is also reported.
ISSN:0141-0229
1879-0909
DOI:10.1016/S0141-0229(98)00165-3