Purification and characterization of novel organic solvent tolerant 98kDa alkaline protease from isolated Stenotrophomonas maltophilia strain SK
| Autor: | Naiem H. Nadaf, Aparna A. Gurav, Shailesh R. Waghmare, D. B. Jadhav, Kailas D. Sonawane, Sonal A. Mali |
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| Rok vydání: | 2015 |
| Předmět: |
Stenotrophomonas maltophilia
Metal ions in aqueous solution Molecular Sequence Data Substrate Specificity chemistry.chemical_compound Bacterial Proteins Endopeptidases Enzyme Stability Ammonium Phylogeny Soil Microbiology chemistry.chemical_classification Chromatography biology Strain (chemistry) Ion exchange Temperature Hydrogen-Ion Concentration biology.organism_classification Enzyme assay Enzyme chemistry Metals biology.protein Bacteria Biotechnology |
| Zdroj: | Protein Expression and Purification. 107:1-6 |
| ISSN: | 1046-5928 |
| Popis: | Ability of microorganisms to grow at alkaline pH makes them an attractive target for several industrial applications. Thus, search for new extremozyme producing microorganisms must be a continuous exercise. Hence, we isolated a potent alkaline protease producing bacteria from slaughter house soil. The morphological, biochemical and 16S rDNA gene sequencing studies revealed that the isolated bacteria is Stenotrophomonas maltophilia strain SK. Alkaline protease from S. maltophilia strain SK was purified by using ammonium sulphate precipitation and DEAE-cellulose ion exchange column chromatography. The purified enzyme was optimally active at pH 9.0 and temperature 40 °C with broad substrate specificity. It was observed that the metal ions such as Ca++, Mg++ and Fe+++ completely repressed the enzyme activity. The enzyme was stable in presence of various water miscible solvents like ethanol, methanol, isopropanol at 25% (v/v) concentration and less stable at 37.5% (v/v) concentration. These robust properties of enzyme might be applicable for various applications in detergent and pharmaceutical industries. |
| Databáze: | OpenAIRE |
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