title: Purification and characterization of membrane-bound peroxidase from date palm leaves (Phoenix dactylifera L.).
abstract: 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 55 kDa 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 K m values of 0.77 and 0.045 mM 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.
authors: Biochemistry Department, College of Science, King Saud University, P.O. Box 2454, Riyadh, Saudi Arabia.
authors: Abdurrahman M
authors: AM
authors: Al-Senaidy
authors: Mohammad A
authors: MA
authors: Ismael
keywords: Characterization; Date palm leaves; Peroxidase; Purification; Substrate specificity; Thermostability
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