[Purification and characterization of extracellular halophilic protease from haloarchaea Natrinema sp. R6-5].
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.
Shi
Wan-liang
WL
College of Life Science, Wuhan University, Wuhan 430072, China. shiwl@eyou.com
Zhong
Chuan-qi
CQ
Tang
Bing
B
Shen
Ping
P
D006216:Halobacteriaceae / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D012965:Sodium Chloride / Q000494:pharmacology; D013696:Temperature
D012965:Sodium Chloride; D010447:Peptide Hydrolases