Purification and characterization of peroxidase from Moringa Oleifera L. Leaves
作者： Ahmad Rosma , Shahanaz Khatun , Farzana Pervin , Nurul Absar , Md. Rezaul Karim
DOI: 10.15376/BIORES.7.3.3237-3251
关键词:
摘要: Peroxidase catalyzes the oxidation of various electron donor substrates such as phenol and aromatic amines in presence hydrogen peroxide. In this study, peroxidase was purified 164-fold from leaves Moringa oleifera L. with a recovery 28% by ammonium sulphate precipitation, DEAE-cellulose column chromatography, Sephadex G-200 Con-A chromatography. SDS-PAGE showed polypeptide band molecular weight 43 kDa. The enzyme found to be single subunit nature. displayed optimum activity at pH 6.0 temperature 50 °C Km value 0.2335 mM for guaiacol best substrate. It is glycoprotein that contains 9.05% sugar estimated sulfuric acid method. Some ions (Ni2+, Pb2+, Zn2+, Al3+, Mg2+, Cu2+, Co2+, Cd2+) exhibited low inhibitory effect while Fe2+, Fe3+, Hg2+ strong effects. EDTA markedly inhibited activity.
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