Purification, characterization and thermodynamics of antifungal protease from Streptomyces sp. A6.

@article{Singh2011PurificationCA,
  title={Purification, characterization and thermodynamics of antifungal protease from Streptomyces sp. A6.},
  author={Anil Kumar Singh and Hari S. Chhatpar},
  journal={Journal of basic microbiology},
  year={2011},
  volume={51 4},
  pages={424-32}
}
A 20 kDa antifungal serine protease from Streptomyces sp. A6 was purified to 34.56 folds by gel permeation chromatography. The enzyme exhibited highest activity at neutral to near alka- line pH 7-9 and 55 °C. Neutral surfactant triton X-100 enhanced the activity by 4.12 fold. The protease activity also increased (109.9-119%) with increasing concentration of urea (2-8 mole/l). The enzyme was identified as serine protease with 67% similarity to SFase 2 of Streptomyces fradiae by MALDI-LC-MS/MS… CONTINUE READING

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