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Peroxidases being one of the key antioxidant enzymes are involved in the essential physiological process. They play an essential role in medicinal, biochemical, industrial and environmental applications. They can catalyse degradation/transformation of aromatic dyes either by precipitation or by opening the aromatic ring structure. Radish being the source of peroxidase have been employed for the remediation of commercial dyes. Pure Radish extract was prepared by adding buffers and proteins were precipitated. The enzyme was dialysed, assayed and characterized for the optimum pH and temperature. The protein was fractionated using SDS-PAGE electrophoresis to find the approximate molecular weight. The optimum pH for peroxidase activity was found to be 5.8. The optimum temperature for peroxidase activity was found to be 50°C The molecular weight of the partially purified peroxidase enzyme is 43kDa. The study proves that with further advancement in purification method these plant peroxidase can be used as a potential source for various biotechnological applications.
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