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Asian Journal of Biochemistry
  Year: 2012 | Volume: 7 | Issue: 3 | Page No.: 123-132
DOI: 10.3923/ajb.2012.123.132
Purification and Characterization of Extracellular Protease from Halotolerant Bacterium Virgibacillus dokdonensis VITP14
V. Devi Rajeswari, G. Jayaraman and T.B. Sridharan

Abstract:
In this study extracellular protease was purified with ammonium sulphate precipitation, dialysis, gel filtration and ion exchange chromatography. The purity was checked with MALDI-TOF and SDS-PAGE. Confirmation of protease was done with zymogram. The molecular weight of the protease was found to be 36 kDa. MALDI-TOF analysis of the protein showed the Molecular weight confirmation of the studied protease. Further the enzyme was characterized for its maximal activity with different pH, temperature, salt concentration and inhibitors. The maximal activity was found at pH 7.0, 40°C, 1.5 M salt concentration and found to be serine protease.
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How to cite this article:

V. Devi Rajeswari, G. Jayaraman and T.B. Sridharan, 2012. Purification and Characterization of Extracellular Protease from Halotolerant Bacterium Virgibacillus dokdonensis VITP14. Asian Journal of Biochemistry, 7: 123-132.

DOI: 10.3923/ajb.2012.123.132

URL: https://scialert.net/abstract/?doi=ajb.2012.123.132

 
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