Laccases are multicopper oxidases, produced majorly by fungal species and are commonly used for dye degradation, bioremediation, waste detoxification and delignification. This study was performed to produce, optimize, purify and to analyse the degrading ability of the enzyme laccase; which is widely known for its high oxidative activity and low substrate specificity. This enzyme can be predominantly found in white-rot fungi and thus was isolated from a fungal species obtained from marine sample. In order to achieve maximal laccase activity, an optimized production medium containing Glucose [10g L−1], MgSO4⋅7H2O [0.1g L −1] and Yeast extract [5g L −1] was used. Laccase formation was also stimulated by optimizing the value of CuSO4[1.0 mM]. Further increase in concentration of CuSO4 proved to be toxic to the organism. The enzyme assay was done in duplicates by using Guaiacol as the substrate in order to determine the enzyme activity. The purified extracellular laccase obtained after Ammonium Sulphate precipitation and DEAE- Cellulose chromatography was subjected to SDS- PAGE and had an apparent molecular mass of 66 kDa. The ability of Laccase to degrade chemical compounds using just molecular Oxygen was assessed through the degradation of Bisphenol-A, an Endocrine Disrupting Chemical.