Bacillus stearothermophilus KP 1236 neutral protease with strong thermostability comparable to thermolysin
| Autor: | Hisataka Taguchi, Yukio Takii, Yuzuru Suzuki, Hidesato Shimoto |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
chemistry.chemical_classification
Metalloproteinase Bacillaceae Chromatography General Medicine Biology biology.organism_classification Applied Microbiology and Biotechnology Bacillales Sedimentation coefficient Isoelectric point Enzyme Biochemistry chemistry Thermolysin Biotechnology Thermostability |
| Zdroj: | Applied Microbiology and Biotechnology. 27 |
| ISSN: | 1432-0614 0175-7598 |
| DOI: | 10.1007/bf00251943 |
| Popis: | An extracellular neutral protease, of Bacillus stearothermophilus KP 1236 (a soil isolate) able to grow at 39°–71°C was purified to homogeneity. The molecular weight, sedimentation coefficient in water at 20°C, and isoelectric point were estimated as 33,000, 3.46 S and 7.5, respectively. The enzyme was most active at 80°C and pH 7.0. The activity was stable for 10 min up to 80°C at pH 7.5 and for 18 h at 60°C over pH 6.0–8.8. The enzyme and thermolysin (microbial metalloproteinase, EC 3.4.24.4) shared their antigenic determinants in part. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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