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Production, Purification and In-silico Characterization of Azoreductase Enzyme Azor1 KF803342 from Pluralibacter gergoviae Involved in Dye Degradation | Abstract
ISSN: 2155-6199

Journal of Bioremediation & Biodegradation
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Research Article

Production, Purification and In-silico Characterization of Azoreductase Enzyme Azor1 KF803342 from Pluralibacter gergoviae Involved in Dye Degradation

Megha K Purohit and Piyush V Desai*
Department of Biosciences, Veer Narmad South Gujarat University, Surat, India
Corresponding Author : Piyush V Desai
Department of Biosciences
Veer Narmad South Gujarat University
Gujarat, India
Tel: +91 281-2586419
E-mail: [email protected]/ [email protected]
Received January 02, 2014; Accepted February 21, 2014; Published February 26, 2014
Citation: Purohit MK, Desai PV (2014) Production, Purification and In-silico Characterization of Azoreductase Enzyme Azor1 KF803342 from Pluralibacter gergoviae Involved in Dye Degradation. J Bioremed Biodeg 5:217. doi:10.4172/2155-6199.1000217
Copyright: © 2014 Purohit MK, et al. This is an open-a ccess article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Abstract

Azo dyes are a wide spread class of poorly biodegradable industrial pollutants.The process of optimization of degradative potential is certainly a challenging task for its industrial applicability. In our current studies; we tried to understand whether azoreductases enzyme plays a significant role in textile dye degradation process.

Optimization of media for maximum degradation by response surface methodologywould certainly boost cleanup of dye pollutants. Further, getting insight into the azoreductase enzyme properties of the enzyme by purification and insilico approaches would allow us to know the structural and functional properties of enzyme. The azoreductase gene isolated from Pluralibacter gergoviae was amplified and sequenced; it showed partial homology to an azoreductase identified in Cronobacter sp. The identity of the enzyme was confirmed by sequencing of azoreductase gene. The nucleotide sequence of enzyme was submitted to Gene bank, accession number-KF803342. The structure of azoreductase was modeled having four FMN binding site. This research provides insight into the use of response surface methodology to rapidly optimize dye biodegradation parameters.

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