Purification and biochemical characterization of the haloalkaliphilic archaeon Natronococcus occultus extracellular serine protease.

@article{Studdert2001PurificationAB,
  title={Purification and biochemical characterization of the haloalkaliphilic archaeon Natronococcus occultus extracellular serine protease.},
  author={Claudia Alicia Studdert and Mar{\'i}a Karina Herrera Seitz and M I Plasencia Gil and Jorge J. Sanchez and Rosana Esther de Castro},
  journal={Journal of basic microbiology},
  year={2001},
  volume={41 6},
  pages={375-83}
}
A serine protease was purified from Natronococcus occultus stationary phase culture medium (328-fold, yield 19%) and characterized at the biochemical level. The enzyme has a native molecular mass of 130 kDa, has chymotrypsin-like activity, is stable and active in a broad pH range (5.5-12), is rather thermophilic (optimal activity at 60 degrees C in 1-2 M NaCl) and is dependent on high salt concentrations for activity and stability (1-2 M NaCl or KCl). Polyclonal antibodies were raised against… CONTINUE READING

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