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Aim: This study was aimed at the isolation, partial purification and characterization of peroxidase from low cost material, Calotropis procera leaves.
Materials and Methods: Partial purification of crude enzyme extract was done by ammonium sulfate precipitation followed by dialysis against Tris-HCl buffer. Peroxidase activity was measured spectrophotometrically.
Results: It was observed that after partial purification, the enzyme specific activity was increased as compared to crude enzyme extract. Peroxidase from Calotropis procera leaves was purified up to 2.04 fold with specific activity of 2.68 U/mg after dialysis. The partially purified peroxidase displayed optimum activity at temperature 50°C and pH 6.0. The kinetic data shows that guaiacol is a better substrate than ABTS. All the tested metal ions (Fe3+, Co2+, Ni2+, Mg2+, Zn2+) and EDTA exhibited strong inhibitory effects on the Calotropis procera leaves peroxidase.
Conclusion: It is more evident that Calotropis procera leaves are a good source of peroxidase. It is therefore, concluded that further purification and full biochemical characterization of this enzyme may serve as a promising option to be explored for industrial purposes.