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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...

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PMID: 17163509
DOI: 10.1002/bit.21292

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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