Purification and characterization of a thermostable serine protease from Bacillus thuringiensis
| Autor: | Iwao Ohmori, Akane Kunitate, Masaji Okamoto |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
Serine protease
chemistry.chemical_classification Gel electrophoresis Protease biology Chemistry medicine.medical_treatment biology.organism_classification General Biochemistry Genetics and Molecular Biology Serine Isoelectric point Enzyme Biochemistry Bacillus thuringiensis biology.protein medicine General Agricultural and Biological Sciences Thermostability |
| Zdroj: | Agricultural and Biological Chemistry. 53:3251-3256 |
| ISSN: | 1881-1280 0002-1369 |
| DOI: | 10.1271/bbb1961.53.3251 |
| Popis: | Bacillus thuringiensis var. kurstaki Hd-255 was found to produce an extracellular, thermostable protease after the end of the vegetative growth phase. The purified enzyme had a molecular weight of 34,000 according to sodium dodecyl sulfate-polyacrylamide gel electrophoresis and an isoelectric point of 9.0.Its proteolytic activity was inhibited by an active-site inhibitor of serine protease, phenylmethyl-sulfonyl fluoride, and also by an SH-modifying reagent, p-chloromercuribenzoic acid, suggesting that the enzyme is one of a subfamily of SH-containing serine proteases.The enzyme showed maximal proteolytic activity at 70°C and pH 8.5 ~ 9. The most interesting characteristic was its thermostability; it retained 88.4 % of its initial activity at pH 8.7 and 60°C after more than 7 hr incubation in the presence of 2mm CaCl2. |
| Databáze: | OpenAIRE |
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