Studies on peroxidase from Moringa oleifera Lam leaves
Oluwadare Joel Agunbiade, Oladoyin Grace Famutimi, Fatimah Adeola Kadiri, Olakunle Abiodun Kolapo, Isaac Olusanjo Adewale
Abstract
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 °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.
Topics & Concepts
MoringaPeroxidaseSephadexSize-exclusion chromatographyCaffeic acidChemistryChromatographyEnzymeBiochemistryFood scienceAntioxidantMoringa oleifera research and applicationsPhytochemistry and Bioactivity Studies