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- W1878381608 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." @default.
- W1878381608 created "2016-06-24" @default.
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- W1878381608 date "2012-06-07" @default.
- W1878381608 modified "2023-10-16" @default.
- W1878381608 title "Purification and characterization of peroxidase from Moringa oleifera L. leaves" @default.
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- W1878381608 doi "https://doi.org/10.15376/biores.7.3.3237-3251" @default.
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