ABSTRACT
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 9503.3â¯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 40â¯kDa monomeric structure and presented high thermostability, as it was entirely stable at 55⯰C for 30â¯min and retained approximately 13.6% of its activity at 85⯰C. The optimal pH exhibited a broad value range (pHâ¯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 8â¯weeks, and upon recycling for up to 15 uses. Arabian balsam peroxidase appears to be candidate for industrial applications.