Article
Thermostability enhancement and change in starch hydrolysis profile of the maltohexaose-forming amylase of Bacillus stearothermophilus US100 strain.
The Biochemical journal - 15 Feb 2006
Ben Ali Mamdouh, Khemakhem Bassem, Robert Xavier, Haser Richard, Bejar Samir
Abstract excerpt
The implications of Asn315 and Val450 in the atypical starch hydrolysis profile of Bacillus stearothermophilus Amy (a-amylase) US100 have been suggested previously [Ben Ali, Mhiri, Mezghani and Bejar (2001) Enzyme Microb. Tech. 28, 537-542]. In order to confirm this hypothesis, three mutants were generated. Of these two have a single mutation, N315D or V450G, whereas the third contains both mutations. Analysis of...
Topics
- Amino Acid Substitution
- Amylases
- Calcium
- Enzyme Stability
- Geobacillus stearothermophilus
- Hot Temperature
- Hydrolysis
- Models, Molecular
- Mutation
- Oligosaccharides
- Protein Structure, Tertiary
- Starch