Oxidant and solvent stable alkaline protease from Aspergillus flavus and its characterization
Autor: | Kumar Yadav Santosh, Bisht Deepali, null Shikha, null N, Singh Darmwal an |
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Předmět: |
chemistry.chemical_classification
Serine protease Chromatography Protease biology Bran Chemistry medicine.medical_treatment Aspergillus flavus biology.organism_classification Applied Microbiology and Biotechnology Solvent chemistry.chemical_compound Enzyme Solid-state fermentation Alkaline protease solid state fermentation PMSF organic solvent Genetics medicine biology.protein PMSF Agronomy and Crop Science Molecular Biology Biotechnology |
Zdroj: | Scopus-Elsevier African Journal of Biotechnology; Vol 10, No 43 (2011); 8630-8640 |
ISSN: | 1684-5315 |
Popis: | The increase in agricultural practices has necessitated the judicious use of agricultural wastes into value added products. In this study, an extracellular, organic solvent and oxidant stable, serine protease wasproduced by Aspergillus flavus MTCC 9952 under solid state fermentation. Maximum protease yield was obtained when the strain was grown under wheat bran and corn cob mixture (1:1) incubated for 48 h at pH 9.0 and temperature 37°C with 50% of initial moisture content. The partially purified enzyme showed wide range of pH optima (8.0-12.0) and pH stability (7.0-12.0), whereas, optimum temperature was 40°C and was stable over a wide range of temperature 30-45°C. The protease was extremely stable towards several organic solvents. The enzyme retained 80% of its original activity in the presence of non ionic and ionic surfactants and 100% with 10% H2O2 after 1 h of incubation at 30°C. In addition, the enzyme showed excellent compatibility with some commercial powder detergents. The compatibility of our protease with several detergents, oxidants and organic solvents suggests its possible use in detergent industry and peptide synthesis.Key words: Alkaline protease, solid state fermentation, PMSF, organic solvent. |
Databáze: | OpenAIRE |
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