Purification and characterization of extracellular halophilic protease from haloarchaea Natrinema sp.R6-5
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Key Project of National Programs for Fundamental Research and Development of hina (2004CB719600)

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    Abstract:

    A halophilic extracellular protease from a halophilic archaea Natrinema sp. R6-5 was purified to SDS-PAGE homogeneity using bacitracin-Sepharose 4B chromatography. A molecular mass of the purified protease subunit was 62KD determined by SDS-PAGE. The protease activity was inhibited by phenylmethylsulfonyl fluoride (PMSF), suggesting that the protease belong to serine protease. The protease exhibited optimum NaCl concentration is 3 mol/L. At the 3 mol/L NaCl concentration, the optimum temperature and the optimum pH were 45℃ and 8.0. The protease could keep high activity and stability in high salt environment and had potential application value.

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SHI Wan-liang, ZHONG Chuan-qi, TANG Bing, SHEN Ping. Purification and characterization of extracellular halophilic protease from haloarchaea Natrinema sp. R6-5. [J]. Acta Microbiologica Sinica, 2007, 47(1): 161-163

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History
  • Received:May 08,2006
  • Revised:July 05,2006
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