Comparative Studies on the Properties of Peroxidase Partially Purified from Different Parts of Carica papaya
Peroxidase (E.C.1.11.1.7) is an enzyme with wide industrial and biotechnological applications. However, the high cost of commercially available peroxidase places a barrier to its utilization in so many places in the world. Carica papaya Linn. (Pawpaw) has been known as a good source of peroxidase. This study was aimed at identifying the part of papaya with the highest concentration of peroxidase. Peroxidase was extracted from different parts (fruit, leaf and stem) of papaya plant and partially purified through ammonium sulphate precipitation. Peroxidase activity was measured as the change in absorbance due to the oxidation of O-dianisidine in the presence of H2O2. The Vmax and Km were determined from Lineweaver-Burk plot. Highest peroxidase activity was observed after ammonium sulphate precipitation at 60%, 50% and 70% for the fruit, leaf and stem, respectively. The pH and temperature optima for peroxidase were found to depend on the part of the plant: fruit (pH 6.5, 60°C), leaf (pH 7.0, 40°C) and stem (pH 5.5, 70°C). Peroxidase activity in the leaf (38.4 U/ml) was found to be higher than in the stem (8.6 U/ml) and the unripe Carica papaya fruit (0.74 U/ml). From the Lineweaver-Burk plot, peroxidase from the fruit had larger Vmax and Km values (Vmax = 0.678 µmol/min, Km = 0.63 µmol/min) than both from the leaf (Vmax = 0.77 µmol/min, Km = 0.57 µmol/min) and the stem (Vmax = 0.608 µmol/min, Km = 0.171). Hence, the leaf of Carica papaya can serve as cheap source of peroxidase for industrial application.
Enzyme Activity, Biotechnology, Peroxidase, Bioremediation, Lipid Peroxidation, Catalysts
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