Laccases are oxidoreductases known as blue copper proteins as they contain copper atoms in their core structure.They catalyze oxidation of a variety of diphenols, polyphenols, amines, and polyaromatic hydrocarbons and simultaneously reduce molecular oxygen to water. These blue copper oxidases are widely disseminated among fungi, bacteria, insects and higher plants. The use of these ‘ecofriendly’ enzymes spans from paper and pulp industry to food applications and from textile industries to bioremediation processes as they have broad substrate specificity. In this project laccase was produced by Pleurotus ostreatus IBL-02 utilizing lignocellulosic waste material, wheat straw under pre-optimized conditions in solid state fermentation (SSF). Maximum yield (519.44 U/mL) along with 201.33 U/mg of specific activity was monitored in crude extract. The enzyme was then purified (3.4-fold) through a series of processes like ammonium sulfate precipitation, dialysis, ion-exchange chromatography by DEAE-Cellulose and gel filtration by Sephadex G-100. 67 kDa single band was observed by SDS-PAGE. Purified laccase was modified by various immobilization techniques like adsorption, encapsulation, covalent bonding and self cross-linking. Soluble and immobilized laccases was characterized via kinetic studies to analyze the consequence of temperature, substrate concentrations and pH on their activities. The presence of laccase in immobilized beads was confirmed by the use of Energy Dispersive X-ray (EDX) analysis. Native and immobilized enzyme were also utilizsed in different industrial applications like degradation of synthetic dyes, bio-remediation of dye based textile effluents and bio-stoning of denim jeans. The immobilized laccase showed better thermo-stability, reusability and sustainability during different environmental and industrial applications. The modified laccase as demonstrated to be an efficient dye decolorizer.