Peroxidase are heme or non heme containing oxidoreductase enzyme, usually found in plants, animals and microorganisms. They play an important role in the biodegradation of environmental pollutants such as phenolic compound, polyaromatic hydrocarbons, pesticides, herbicides etc. Since, the uses of commercially available peroxidases are highly expensive, it is necessary to develop a readily abundant alternate source with high stability and low cost. That's why, now a days peroxidases are being isolated from different plant sources. In this study, peroxidase was isolated, characterized and purified from radish (Raphanus Sativus) and checked its activity for biotransformation of phenolic compounds. Radish is a good source of peroxidase having activity 4.74 U/mL. The enzyme was purified to homogeneity. The calculated pH optimum, temperature optimum and ionic strength for radish peroxidase were found to be 5.0 ± 0.05, 35 °C and 40 mM. The km value for guaiacol and H2O2 were found to be 0.35 mM and 0.18 mM respectively. Since the Central Pollution Control Board of India (CPCB) and United states Environmental Protection Agency (USEPA) have included cresols as the environment polluting agent in their priority pollutant list. In order to remove this pollutant several physico-chemical treatments have been developed. In this study, the degradation of cresols by radish peroxidase were analyzed by UV-spectroscopy, thin layer chromatography, cyclic voltammetry and GCMS technique. The GCMS analysis confirmed that the radish peroxidase can efficiently degrade o-cresol, m-cresol and p-cresol to a less harmful product at low cost and eco-friendly way.