In silico insights into anthraquinone dye degradation by Flavobacterium sp. 9AF peroxidase and hydrolase

Anthraquinone dyes are extensively used in the textile, cosmetic, and food industries because of their bright colors, stability toward chemicals, and resistance against fading. Yet their large-scale application has resulted in great environmental problems. Anthraquinone dyes are extremely recalcitrant, that is, resistant to natural degradation processes, and have toxic impacts on aquatic life and human health. Traditional dye removal methods like adsorption and chemical oxidation tend to be inefficient and expensive, which has necessitated novel approaches. Enzymatic bioremediation is a novel method that has gained popularity due to its sustainability and high catalytic efficiency. This research examines the potential of two enzymes from Flavobacterium sp. 9AF—Putative Multifunctional Dye Peroxidase DyP2 and Glycoside Hydrolase Family 5 Protein—to perform degradation through in silico approaches. Molecular docking showed that DyP2 has greater binding affinities for Solvent Green 3 (−12.1 kcal/mol), Vat Blue 6 (−11.4 kcal/mol), and Reactive Blue 19 (−11.3 kcal/mol) than Glycoside Hydrolase Family 5 Protein. Interaction analysis showed that DyP2 has stronger hydrogen and hydrophobic bonds with pollutants, indicating its better catalytic ability for dye degradation. These results present DyP2 as an attractive biocatalyst for remediation of anthraquinone dye, which has potential for enzyme-based applications in industrial wastewater treatment and conservation.