Partial purification of peroxidase from kailan (Brassica oleraceae var Alboglabra) by micro- and ultrafiltration membrane.

Peroxidase enzymes are a group of oxidoreductase enzymes that catalyse the reduction of peroxides such as hydrogen and oxidise organic and inorganic compounds. Membrane processing is a promising alternative technology for the separation and purification of enzymes. This study partially purified peroxidase from Kailan (Brassica oleraceae var Alboglabra) by micro-and ultrafiltration membrane technology. The effects of physicochemical conditions (pH and temperature) on peroxidase were examined, and the purity and enzyme activity of resulted peroxidase was also determined. The crude peroxidase enzyme isolated from Kailan was passed through a microfiltration membrane (0.15 µm) with pressure 40 psia, rotation speed 400 rpm, and a flow rate of 30 mL/min, followed by an ultrafiltration module with the pressure of 40 psia and rotation speed 200, 300 and 400 rpm at room temperature. The optimum pH and temperature of peroxidase were pH 6.0 and 27 °C, respectively, as determined with guaiacol as the substrate. The purification of peroxidase by micro-and ultrafiltration process at optimum conditions resulted in specific activity of 392.16 and 749.91 U/mg with a purity level of 5.20 and 9.95 fold than crude enzyme activity. Thus, the membrane technology has a potential purification method for peroxidase production. [ABSTRACT FROM AUTHOR]