Article
The stability of engineered thermostable neutral proteases from Bacillus stearothermophilus in organic solvents and detergents.
Biotechnology and bioengineering - 1 Jul 2007
Mansfeld Johanna, Ulbrich-Hofmann Renate
Abstract excerpt
Engineered extremely thermostable variants of the thermolysin-like protease from Bacillus stearothermophilus possessing an introduced disulfide bond G8C/N60C (double mutant, DM) and six additional amino acid substitutions in the exposed loop region 56-69 (Boilysin, BLN) have been probed with respect to stability toward water-miscible organic solvents and detergents. The solvent concentrations where 50% of enzyme...
Topics
- Amino Acid Sequence
- Amino Acid Substitution
- Detergents
- Disulfides
- Dose-Response Relationship, Drug
- Enzyme Stability
- Genetic Variation
- Geobacillus stearothermophilus
- Molecular Sequence Data
- Organic Chemicals
- Peptide Hydrolases
- Protein Engineering
- Protein Structure, Secondary
- Solvents
- Temperature
- Water