Peroxidase from date palm (Phoenix dactylifera L.) leaves was purified to homogeneity and characterized biochemically. The enzyme purification included homogenization, extraction of pigments followed by consecutive chromatographies on DEAE-Sepharose and Superdex 200. The purification factor for purified date palm peroxidase was 17 with 5.8% yield. The purity was checked by SDS and native PAGE, which showed a single prominent band. The molecular weight of the enzyme was approximately 55kDa as estimated by SDS-PAGE. The enzyme was characterized for thermal and pH stability, and kinetic parameters were determined using guaiacol as substrate. The optimum activity was between pH 5-6. The enzyme showed maximum activity at 55°C and was fairly stable up to 75°C, with 42% loss of activity. Date palm leaves peroxidase showed Kmvalues of 0.77 and 0.045mM for guaiacol and H2O2, respectively. These properties suggest that this enzyme could be a promising tool for applications in different analytical determinations as well as for treatment of industrial effluents at low cost. © 2011.
Al-Senaidy, A. M., & Ismael, M. A. (2011). Purification and characterization of membrane-bound peroxidase from date palm leaves (Phoenix dactylifera L.). Saudi Journal of Biological Sciences, 18(3), 293–298. https://doi.org/10.1016/j.sjbs.2011.04.005