Production and purification of peroxidase from aspergillus niger

Abstract EN

This study was conducted in the laboratories of Biology Department, College of Science, which deals with isolation and purification of peroxidase and optimization of process parameters to achieve maximum yield of peroxidase by Aspergillus niger.

Solid-state fermentation of Aspergillus niger was carried out for enhanced production of peroxidase using hydrogen peroxide as the substrate of enzyme maximum activity of the enzyme was achieved under optimum growth conditions.

The optimum conditions were the isolated of Aspergillus niger from soil and growth in synthetic medium, it gave high titer of peroxidase activity, the fructose as carbon source, peptone as nitrogen source, after 12 days of incubation, incubation temperature 25 °C and pH = 6.5.

Peroxidase purified in four purification steps; precipitation with 70% saturation of ammonium sulfate, step of dialysis, the third by ion exchange chromatography using DEAE-Cellulose and fourth by gel filtration throughout Sephadex G-100.

The specific activity of the purified enzyme was 150U/mg with 7.75 folds.

The peroxidase was shown to have molecular weight of 40kDa in SDS-PAGA and about 40kDa in gel filtration.The optimum pH and temperature for peroxidase activity 7 and 35 C0 respectively.-