A novel peroxidase from Arabian balsam (Commiphora gileadensis) stems: Its purification, characterization and immobilization on a carboxymethylcellulose/Fe3O4 magnetic hybrid material.


Department of Biochemistry, Faculty of Science, University of Jeddah, P.O. Box 80203, Jeddah 21589, Saudi Arabia; Chemistry Department, Faculty of Applied Science, Taiz University, Taiz, Yemen. Electronic address: [Email]


A novel plant peroxidase was isolated from the stem of Arabian balsam (Commiphora gileadensis) and purified using ammonium sulfate, followed by ion exchange chromatography (DEAE-Sepharose) and gel filtration (Sephcryl S-200). The newly isolated peroxidase was characterized as having a specific activity of 9503.3 unit/mg of protein after 20.3-fold purification, which yielded a recovery of 18.5%. Based on the subunit size, the purified peroxidase was a 40 kDa monomeric structure and presented high thermostability, as it was entirely stable at 55 °C for 30 min and retained approximately 13.6% of its activity at 85 °C. The optimal pH exhibited a broad value range (pH 7.0- 7.5). The kinetic parameters for the purified peroxidase were obtained. To increase the enzyme durability, efficiency and reusability, the peroxidase was entrapped onto a carboxymethyl cellulose/Fe3O4 magnetic hybrid material. The immobilized enzyme was characterized by scanning electron microscopy (SEM) and FT-IR spectroscopy. It was tested at different pH values, storage times and temperatures, and its kinetic behavior was assessed. The immobilized enzyme maintained its activity upon storage at 4 and 25 °C for 8 weeks, and upon recycling for up to 15 uses. Arabian balsam peroxidase appears to be candidate for industrial applications.


Arabian balsam,immobilization,peroxidase,purification,scanning electron microscopy,

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