Purification and Properties of an Extracellular Halophilic Serine-Protease from Haloferax mediterranei
Na+, K+, and Mg+2 ions are essential for Haloferax mediterranei growth and extra-cellular protease production. Ammonium ions (> 2 % w/v) reduce enzyme production, whereas Ca+2 ions (~10 mM) enhance it and, in addition, activate the enzyme. The extra-cellular enzyme purified by ultra-filtration and Hydrophobic Interaction Chromatography, consists of a single polypeptide chain of MW 26 500 Da, with optimum activity at 3 M NaCl and pH 8 within 45 to 50 °C. This enzyme belongs to the serine-protease class and could be useful in a variety of industrial applications.
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| Main Authors: | , , |
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| Format: | Digital revista |
| Language: | English |
| Published: |
Sociedad Química de México A.C.
2002
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| Online Access: | http://www.scielo.org.mx/scielo.php?script=sci_arttext&pid=S0583-76932002000300004 |
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| Summary: | Na+, K+, and Mg+2 ions are essential for Haloferax mediterranei growth and extra-cellular protease production. Ammonium ions (> 2 % w/v) reduce enzyme production, whereas Ca+2 ions (~10 mM) enhance it and, in addition, activate the enzyme. The extra-cellular enzyme purified by ultra-filtration and Hydrophobic Interaction Chromatography, consists of a single polypeptide chain of MW 26 500 Da, with optimum activity at 3 M NaCl and pH 8 within 45 to 50 °C. This enzyme belongs to the serine-protease class and could be useful in a variety of industrial applications. |
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