Research article

Investigation Activity and Stability of Peroxidase Plant Enzyme to Decolorize Azo Dyes

Aula I. Ridha* and Mohanad J. M-Ridha

Online First: November 08, 2022

The current work aimed to extract purified Peroxidase enzyme from red radish to determine the enzyme's specific activity at the best temperature and pH. The extracted enzyme was used to decolorize some Azo dyes like Congo red, Methyl red, and Methyl orange. The best experimental condition was sodium acetate buffer 0.1 M, pH 6 for buffer solution for peroxidase extraction from red radish with a specific activity of 44414.4 U/mg protein after using 1:2 (V:W) as the extraction ratio. Ion-exchange chromatography on a CM-cellulose column and 0-70 percent (W:V) saturated ammonium sulfate was used; with the enzyme purified process, the Peroxidase enzyme activity was 2913 U/ml, and protein concentration was 0.014 mg/ml, with a specific activity 208071 U/mg protein, a purification fold of 3.5, and a yield of 77%, partially purified Peroxidase. The partially purified Peroxidase's biochemical properties were examined. The maximum removal efficiencies of the azo dyes were 99.8, 42.9, and 50.4% for Congo red, Methyl red, and Methyl orange investigated in this study. The results showed the ability of plant enzymes to treat different kinds of Azo dyes.


Extraction, Peroxidase enzyme, Ion-exchange chromatography, enzyme stability