NC State
BioResources
Khatun, S., Ashraduzzaman, Md., Karim, Md. R., Pervin, F., Absar, N., and Rosma, A. (2012). "Purification and characterization of peroxidase from Moringa oleifera L. leaves," BioRes. 7(3), 3237-3251.

Abstract

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.
Download PDF