In Silico Comparative Analysis of Azo Dye Interactions with Oxidoreductase, Laccase, and Peroxidase from Acinetobacter junii

The textile industry releases significant amounts of azo dyes in aquatic bodies, which rigorously contributes to water pollution. Microorganisms effectively transform organic and inorganic pollutants into the lesser toxic form during the process of bioremediation with the aid of enzymes. Modern technology has exhibited remarkable advancement in last years. The incorporation of omics approach in the field of bioremediation is an exciting venture to research. It will significantly reduce the screening time. Therefore, this study employs a computational strategy to compare the azo dye degrading potential of three prominent enzymes from Acinetobacter junii, i.e. oxidoreductase, laccase, and peroxidase. For this purpose, six azo dyes, Acid violet 7, Acid orange 19, Congo red, disperse red 1, Disperse red 13, and Reactive brilliant red, were considered for the analysis of molecular interactions with the three enzymes. After 3D structure modeling through I-TASSER and validated by RAMPAGE, the enzymes were docked with the azo dyes by using auto dock vina, and their binding energies and molecular interactions were evaluated. The comparative analysis of enzymes-dye complexes revealed that both oxidoreductase and laccase formed highly stable complexes withall azo dyes, showing strong binding affinities (>-5kcal/mol). Moreover, NAMD used for the molecular dynamic simulations have revealed the minimum conformational deviations for oxidoreductase and laccase compared to the docked complex of peroxidase. These findings suggest that oxidoreductase and laccase of A.junii are highly promising for efficient remediation of toxic azo dyes. However, these enzyme s need further experimental characterization before their use in large-scalem setups.