Purification of lysozyme from chicken egg white using triazine dye affinity method: Performance evaluation and...

Lysozyme is a hydrolytic enzyme with broad industrial applications. In this study, we explored the adsorption of lysozyme onto five triazine-based ligands (Reactive Red 195, Reactive Blue 222, Reactive Yellow 145, Reactive Yellow 160, and Reactive Red 222) immobilized on Sepharose resins. The activated resins were functionalized with 1,4-diaminobutane to facilitate dye immobilization, and successful ligand attachment was confirmed using various characterization techniques. Morphological analysis showed that the resins maintained their spherical structure and uniformity after modification. Adsorption experiments indicated that reactive yellow 160 exhibited the highest adsorption capacity (51.3 mg/mL). Purification of lysozyme from chicken egg white (CEW) demonstrated high recovery efficiency, with reactive red 222 achieving the best performance (93.77 % recovery, 16.24-fold purification). Molecular docking analysis supported these findings by revealing strong binding affinities between lysozyme and the triazine-based ligands, with binding energies ranging from -8.3 to -10.3 kJ/mol. Overall, this approach is highly effective and shows strong potential for large-scale lysozyme isolation in industrial applications.