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International Journal of Pure & Applied Bioscience (IJPAB)
Year : 2016, Volume : 4, Issue : 4
First page : (238) Last page : (243)
Article doi: http://dx.doi.org/10.18782/2320-7051.2341

Purification and Characterization of Azoreductase from B. licheniformis

K. Suganya and K. Revathi*
PG and Research Department of Zoology, Ethiraj College for Women, Chennai, India
*Corresponding Author E-mail: reva63@rediffmail.com
Received: 27.07.2016  |  Revised: 10.08.2016   |  Accepted: 12.08.2016  

Dye decolorizing bacteria was isolated and identified from textile effluent samples. The isolate was identified as Bacillus licheniformis by 16S rDNA sequencing. Azoreductase, an enzyme responsible for catalyzing the reductive cleavage of azo bonds was purified from B.licheniformis. The enzyme was purified by a combination of ammonium sulphate precipitation, ion exchange and affinity chromatography. The optimum pH and temperature of purified enzyme was found to be 7 and 20ºC. The molecular mass of purified enzyme determined by SDS-PAGE was found to be 18 kDa.

Key words: Azoreductase, B.licheniformis, optimization, purification.

Full Text : PDF; Journal doi : http://dx.doi.org/10.18782

Cite this article: Suganya, K. and Revathi, K., Purification and Characterization of Azoreductase from       B. licheniformis, Int. J. Pure App. Biosci.4(4): 238-243 (2016). doi: http://dx.doi.org/10.18782/2320-7051.2341