Studies on peroxidase from Moringa oleifera Lam leaves

Kinetic and physicochemical properties of Moringa oleifera peroxidase purified using a novel and cost efficient protocol was investigated with a view to providing information on its possible biotechnological potentials. Moringa oleifera peroxidase was purified to homogeneity in two steps, involving ATPS and size exclusion chromatography on Sephadex G-100 with a yield of 84.12 %. In-gel activity staining revealed the presence of one isoform of peroxidase. The purified peroxidase is monomeric with native and subunits molecular weight of 38.9 and 43.5 kDa respectively. Kinetic parameters - V-max, K-m(app)(o-dianisidine) (,) K-m(app)(H2O2) of the purified enzyme were 2.5 units/mg protein, 0.020 +/- 0.04 mM and 1.37 +/- 0.18 mM respectively. Its optimum pH and temperature were 5 and 30 degrees C respectively. The purified enzyme cross-linked BSA into an insoluble matrix with the aid of caffeic acid. The study concluded that the purification scheme adopted is rapid and efficient, the purified enzyme exhibited some physiochemical properties that make it suitable for various biotechnological applications.

Automated summary

The study investigated the kinetic and physicochemical properties of Moringa oleifera peroxidase purified using a cost-effective protocol. The purified enzyme exhibited monomeric structure, optimum pH of 5, and optimum temperature of 30 degrees Celsius, showing potential for various biotechnological applications.