The stability of engineered thermostable neutral proteases from Bacillus stearothermophilus in organic solvents and detergents.

@article{Mansfeld2007TheSO,
  title={The stability of engineered thermostable neutral proteases from Bacillus stearothermophilus in organic solvents and detergents.},
  author={Johanna Mansfeld and R Ulbrich-hofmann},
  journal={Biotechnology and bioengineering},
  year={2007},
  volume={97 4},
  pages={672-9}
}
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 activity were irreversibly lost (C(50)) decreased in the order methanol > 2… CONTINUE READING

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