The lignin degrading enzymes system of WRF has incredible catalytic property for oxidative bio-remediation of a lot of toxic contaminants and numerous other industrial applications. Immobilization facilitates the re-use of enzymes and making them industrially applicable and eco-nomical bio-catalysts. Schizophyllum commune IBL-06 was used for the production of lignin peroxidase (LiP) in pre-optimized solid state fermentation medium of corn stover. A high yield of LiP (1347.3 U/mL) was observed in crude extract. LiP was purified (5.65 folds) by a 4 steps protocol containing ammonium sulphate fractionation, dialysis, ion-exchange (DEAE-cellulose) and size exclusion chromatography. The 38 kDa single polypeptide S. commune IBL-06 LiP migrating as a single clear band on both native and SDS-PAGE gels. The purified enzyme was then immobilized on different support matrics such as chitosan, alginate, nylon membrane, PVA, agarose and PA gels with high immobilization efficiency and stability. Scanning electron microscopy (SEM) was performed for the verification of LiP attachment on support matrices. The maximum dye-decolorization (95.45%) potential was observed with chitosan and ca-alginate immobilized enzyme at 30°C without hemolytic toxicity. The chitosan beads-LiP retained approximately more than 70% activity after 3 frequent runs that gradually reduced to 35 % after 7th cycle of reusability. The immobilized LiP was found to show superior dye removal properties as compared to free LiP. Higher thermo stability, lower Km and high Vmax features of chitosan beads immobilizedLiP suggested its suitibility for variousbiotechnological and industrial applictaions.