IN-SILICO MOLECULAR MODELLING AND DOCKING STUDIES OF SELECTED TEXTILE DYES AND LACCASE TO INVESTIGATE THE DYE DEGRADATION MECHANISM OF THE ENZYME

Abstract

Among the fungal enzymes, laccases are of great interest, because laccase offer more stability and the possibility to utilize the enzyme in its immobilized form and are able to degrade numerous textile dyes. The aim of this investigation was to characterize the interaction of enzyme laccase from white rot fungus Trametes hirsuta with textile dyes and establish its ability to decolorize textile dyes in industrial effluent. Here the activity of laccase was determined by in-silico method where, the enzyme laccase from Trametes hirsuta was docked using Autodock Vina with dyes such as Reactive blue160, Congo red, Bromophenol blue, Disperse blue 1, Malachite green to characterized the degradation of the dyes by the enzymes using insilico method. The dyes were found to bind to the copper containing T1, T2, and T3 active site bridging with (GLN 237, GLN 242, TYR 244, ASN 262, ARG 423, SER 427, PHE 162, GLN 264, LEU 459, GLU 460, LEU 355) of laccase. Laccase are capable of degrading a wide variety of compounds, and they are commercially significant. This study provides useful information on the mechanism of dye degradation.