Abstract
The Plant peroxidases are remarkable enzymes due to their widespread use in industry. These enzymes, which are capable of catalyzing the oxidation of various organic and inorganic substrates, have been used in clinical diagnosis, detoxification reactions and organic synthesis. In this study, in vitro production and purification of peroxidase enzyme from cauliflower plant was proposed. Firstly, sterile seedlings were obtained from MS/B5 nutrient medium without growth regulator from cauliflower seeds and calluses from medium containing 0.5 mg / L 2.4-D. Callus and seedlings were powdered with liquid nitrogen and then homogenized. Peroxidase enzymes were purified from these homogenates using affinity technique. SDS-PAGE electrophoresis was performed to determine the molecular weight of the purified enzymes and single bands was observed at approximately 46 kDa. In addition, KM and Vmax values of the callus peroxidase enzyme were determined for guaiacol, pyrogallol and H2O2 substrates.
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