Unlocking the power of enzymes: Comparative molecular docking analysis of Escherichia coli enzymes for disperse dye degradation and toxicity mitigation
Abstract
Disperse dyes are synthetic, non-biodegradable pollutants extensively used in textile manufacturing. They pose significant environmental and health risks due to their persistence and toxicity. Traditional treatment methods fail to ensure complete degradation of enzymatic bioremediation. This study aims to evaluate the biodegradation potential of three Escherichia coli enzymes azoreductase, aryl sulfotransferase, and alkanesulfonate monooxygenase, against disperse dye pollutants using computational tools. Protein sequences were retrieved from NCBI and analyzed for physicochemical and structural properties using Expasy ProtParam and SOPMA. Homology models were built via SWISS-MODEL and validated with ERRAT. Twelve disperse dyes from PubChem were selected for molecular docking through CB-Dock2, and interactions were visualized with Discovery Studio. BioTransformer 3.0 predicted the metabolic degradation pathways of the dyes. All three enzymes exhibited stable structures and favorable secondary compositions. Docking results showed strong binding affinities for Disperse Orange 1 with azoreductase (-8.6 kcal/mol), Disperse Red 13 with aryl sulfotransferase (-8.4 kcal/mol), and Disperse Orange 3 with alkanesulfonate monooxygenase (-7.2 kcal/mol), involving hydrogen bonds and hydrophobic interactions. Metabolic predictions suggested enzymatic transformations via hydroxylation and dealkylation. E. coli enzymes, especially azoreductase, demonstrate promising potential for disperse dye biodegradation, supporting their application in sustainable wastewater treatment systems.