Purification and biochemical characterization of a protease secreted by the Salinivibrio sp. strain AF-2004 and its behavior in organic solvents

@article{KarbalaeiHeidari2006PurificationAB,
  title={Purification and biochemical characterization of a protease secreted by the Salinivibrio sp. strain AF-2004 and its behavior in organic solvents},
  author={Hamid Reza Karbalaei-Heidari and Abed-Ali Ziaee and Mohammad Ali Amoozegar},
  journal={Extremophiles},
  year={2006},
  volume={11},
  pages={237-243}
}
A metalloprotease secreted by the moderately halophilic bacterium Salinivibrio sp. strain AF-2004 when the culture reached the stationary growth phase. This enzyme was purified to homogeneity by acetone precipitation and subsequent Q-Sepharose anion exchange and Sephacryl S-200 gel filtration chromatography. The apparent molecular mass of the protease was 31 kDa by SDS-PAGE, whereas it was estimated as approximately 29 kDa by Sephacryl S-200 gel filtration. The purified protease had a specific… CONTINUE READING
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