The intracellular bacterial peroxidase from Pseudomonas sp. SUK1 was purified by anion exchange and molecular sieve chromatography. The molecular weight of the purified peroxidase was estimated to be 86 kDa by SDS-PAGE analysis. The UV-visible absorption spectra revealed that the purified peroxidase was a heme-containing protein. The purified enzyme exerted its optimal activity with n-propanol and also oxidized various lignin-related phenols, whereas no activity was observed with p-cresol and veratrole. Optimum pH and temperature for the purified peroxidase were 3.0 and 40°C, respectively. The purified enzyme proficiently decolorized various textile dyes. Methyl orange was used as a model azo dye to understand the mechanism of action of peroxidase in dye degradation. Further, dye degradation was confirmed by analytical techniques like FTIR, HPLC and GC-MS.