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Abstract Background and objective: PPO enzyme catalyze oxidation of o-diphenol to o-quinone by utilizing oxygen and the final product is undesirable black pigments. Fruits and vegetables are sensitive to enzymatic browning. Several industries produce wastewater containing phenol and its derivatives. Removal of phenols and degradation from wastewater by using enzymes is possible by developing biosensors to detect phenolic compounds. The inhibition of PPO is significant for the preservation of food products, vegetables with good quality and also clinically useful for the treatment of dermatological disorders related to hyperpigmentation also helpful in developing cosmetic products. In view of the applications the present investigation deals with the characterization and inhibition kinetics of PPO from Cinnamomum verum fruit coat. Material and methods: Purification and quantification of an enzyme are done by ammonium sulfate precipitation, dialysis and followed by the sephadex G-100 column chromatography technique. Molecular weight was analyzed by SDS-PAGE. The Km and Vmax were determined from a Lineweaver-Burk plot by following the optimum pH, temperature and freeze-thaw conditions. The effect of