title: [Purification and characterization of extracellular halophilic protease from haloarchaea Natrinema sp. R6-5].
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 degrees C and 8.0. The protease could keep high activity and stability in high salt environment and had potential application value.
authors: College of Life Science, Wuhan University, Wuhan 430072, China. shiwl@eyou.com
authors: Wan-liang
authors: WL
authors: Shi
authors: Chuan-qi
authors: CQ
authors: Zhong
authors: Bing
authors: B
authors: Tang
authors: Ping
authors: P
authors: Shen
mesh_terms: D006216:Halobacteriaceae / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D012965:Sodium Chloride / Q000494:pharmacology; D013696:Temperature
chemical_list: D012965:Sodium Chloride; D010447:Peptide Hydrolases