PURIFICATION AND CHARACTERIZATION OF PEROXIDASE FROM MORINGA OLEIFERA L. LEAVES
2012
Shahanaz Khatun, | Md. Ashraduzzaman, | Md. Rezaul Karim, | Farzana Pervin, | Nurul Absar, | Ahmad Rosma
Peroxidase catalyzes the oxidation of various electron donor substrates such as phenol and aromatic amines in the presence of hydrogen peroxide. In this study, peroxidase was purified 164-fold from the leaves of Moringa oleifera L. with a recovery of 28% by ammonium sulphate precipitation, DEAE-cellulose column chromatography, Sephadex G-200 column chromatography, and Con-A column chromatography. SDS-PAGE showed a polypeptide band with molecular weight of 43 kDa. The enzyme was found to be a single subunit in nature. The purified enzyme displayed optimum activity at pH 6.0 and at a temperature of 50 °C with a Km value of 0.2335 mM for guaiacol as best substrate. It is a glycoprotein that contains 9.05% sugar as estimated by the phenol sulfuric acid method. Some ions (Ni2+, Pb2+, Zn2+, Al3+, Mg2+, Cu2+, Co2+, and Cd2+) exhibited low inhibitory effect while Fe2+, Fe3+, and Hg2+ exhibited strong inhibitory effects. EDTA markedly inhibited the peroxidase activity.
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