Article
A single mutation within a Ca(2+) binding loop increases proteolytic activity, thermal stability, and surfactant stability.
Biochimica et biophysica acta - 1 Mar 2013
Okuda Mitsuyoshi, Ozawa Tadahiro, Tohata Masatoshi, Sato Tsuyoshi, Saeki Katsuhisa, Ozaki Katsuya
Abstract excerpt
We improved the enzymatic properties of the oxidatively stable alkaline serine protease KP-43 through protein engineering to make it more suitable for use in laundry detergents. To enhance proteolytic activity, the gene encoding KP-43 was mutagenized by error-prone PCR. Screening identified a Tyr195Cys mutant enzyme that exhibited increased specific activity toward casein between pH 7 and 11. At pH 10, the mutant...
Topics
- Alkalies
- Amino Acid Sequence
- Amino Acid Substitution
- Bacillus
- Bacterial Proteins
- Binding Sites
- Calcium
- Cysteine
- Enzyme Stability
- Hydrogen-Ion Concentration
- Kinetics