Purification and characterization of a keratinolytic serine protease from <i>Purpureocillium lilacinum</i> LPS # 876
A keratinolytic serine protease secreted by <i>Purpureocillium lilacinum</i> (formerly <i>Paecilomyces lilacinus</i>) upon culture in a basal medium containing 1% (w/v) hair waste as carbon and nitrogen source was purified and characterized. After purification the keratinase...
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| Autores principales: | , , , |
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| Formato: | Articulo Preprint |
| Lenguaje: | Inglés |
| Publicado: |
2013
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| Acceso en línea: | http://sedici.unlp.edu.ar/handle/10915/104353 http://hdl.handle.net/11336/4312 |
| Aporte de: |
| Sumario: | A keratinolytic serine protease secreted by <i>Purpureocillium lilacinum</i> (formerly <i>Paecilomyces lilacinus</i>) upon culture in a basal medium containing 1% (w/v) hair waste as carbon and nitrogen source was purified and characterized. After purification the keratinase was resolved by SDS-PAGE as a homogeneus protein band of molecular mass 37.0 kDa. The extracellular keratinase of <i>P. lilacinum</i> was characterized by its appreciable stability over a broad pH range (from 4.0 to 9.0), and up to 65 °C, along with its strong inhibition by phenylmethylsulphonyl fluoride among the protease inhibitors tested (98.2% of inhibition), thus suggesting its nature as a serine protease. The enzyme was active and stable in the presence of organic solvents such as dimethylsulfoxide, methanol, and isopropanol; certain surfactants such as Triton X-100, sodium dodecylsulfate, and Tween 85; and bleaching agents such as hydrogen peroxide. These biochemical characteristics suggest the potential use of this enzyme in numerous industrial applications. |
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