Purification and Properties of an Extracellular Halophilic Serine-Protease from Haloferax mediterranei
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| Format: | Artículo científico |
| Language: | en |
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Sociedad Química de México
2002
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| _version_ | 1876471223964139520 |
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| author | José Luis Ochoa |
| author_facet | José Luis Ochoa |
| contents | Purification and Properties of an Extracellular Halophilic Serine-Protease from Haloferax mediterranei José Luis Ochoa Héctor Nolasco Donald J. Kushner Multidisciplinaria (Ciencias Naturales y Exactas) protease extracellular serineproteases Haloferax mediterranei Na+, K+, and Mg+2ions are essential for Haloferax mediterraneigrowthand extra-cellular protease production. Ammoniumions (> 2 % w/v) reduce enzyme production, whereas Ca+2ions (~10mM) enhance it and, in addition, activate the enzyme. The extracellularenzyme purified by ultra-filtration and Hydrophobic InteractionChromatography, consists of a single polypeptide chain ofMW 26 500 Da, with optimum activity at 3 M NaCl and pH 8 within45 to 50 °C. This enzyme belongs to the serine-protease class andcould be useful in a variety of industrial applications. 2002 artículo científico 1870-249X https://www.redalyc.org/articulo.oa?id=47546304 en http://www.redalyc.org/revista.oa?id=475 Journal of the Mexican Chemical Society application/pdf Sociedad Química de México Journal of the Mexican Chemical Society (México) Num.3 Vol.46 |
| format | Artículo científico |
| id | redalyc_47546304 |
| institution | Redalyc |
| language | en |
| publishDate | 2002 |
| publisher | Sociedad Química de México |
| spellingShingle | Purification and Properties of an Extracellular Halophilic Serine-Protease from Haloferax mediterranei José Luis Ochoa Multidisciplinaria (Ciencias Naturales y Exactas) protease extracellular serineproteases Haloferax mediterranei Purification and Properties of an Extracellular Halophilic Serine-Protease from Haloferax mediterranei José Luis Ochoa Héctor Nolasco Donald J. Kushner Multidisciplinaria (Ciencias Naturales y Exactas) protease extracellular serineproteases Haloferax mediterranei Na+, K+, and Mg+2ions are essential for Haloferax mediterraneigrowthand extra-cellular protease production. Ammoniumions (> 2 % w/v) reduce enzyme production, whereas Ca+2ions (~10mM) enhance it and, in addition, activate the enzyme. The extracellularenzyme purified by ultra-filtration and Hydrophobic InteractionChromatography, consists of a single polypeptide chain ofMW 26 500 Da, with optimum activity at 3 M NaCl and pH 8 within45 to 50 °C. This enzyme belongs to the serine-protease class andcould be useful in a variety of industrial applications. 2002 artículo científico 1870-249X https://www.redalyc.org/articulo.oa?id=47546304 en http://www.redalyc.org/revista.oa?id=475 Journal of the Mexican Chemical Society application/pdf Sociedad Química de México Journal of the Mexican Chemical Society (México) Num.3 Vol.46 |
| title | Purification and Properties of an Extracellular Halophilic Serine-Protease from Haloferax mediterranei |
| topic | Multidisciplinaria (Ciencias Naturales y Exactas) protease extracellular serineproteases Haloferax mediterranei |
| url | https://www.redalyc.org/articulo.oa?id=47546304 |