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

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.