STUDIES ON PEROXIDASE FROM AFRICAN EGG (SOLANUM AETHEOPICUM) LEAVES
Abstract
The study focuses on the purification and characterization of peroxidase extracted from African Egg Plant, an abundant agricultural waste product. Peroxidase was initially extracted using a phosphate buffer, resulting in a crude enzyme extract with an activity of 51.6 ± 2.0 units/ml and a protein concentration of 0.86 ± 0.1mg/ml;. the purification process employed an aqueous two phase (ATPS), achieving a specific specificity of 246.5 ± 4 units/mg protein, a yield of 56%, and a purification fold of 4.1. The enzyme was then characterized which involved kinetic parameter, effect of pH, effect of temperature and effect of metals. The enzyme exhibited optimal activity at pH 7.0 and 60’C, maintaining stability across a temperature range of 20-60’C and a pH range of 5.0-7.0. kinetic analysis revealed Km values of 4.5- ± 0.2 Mm for catechol and 8.1 ± 0.1 Mm for hydrogen peroxide, with a Vmax of 356.6 ± 14 units/mg protein. These findings suggest that African Egg leaves peroxidase has significant potential for industrial applications due to its stability and efficiency. The study highlights the feasibility of utilizing African Egg leaves as a cost-effective and sustainable source of industrial enzymes.
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