EXTRACTION, PURIFICATION OF PEROXIDASE FROM PLEUROTOUS TUBEREGIUM A RESEARCH PROJECT

This study focuses on the extraction and purification of peroxidase from Pleurotus tuberregium, a remarkable species of edible mushroom with potential biotechnological applications. Peroxidase enzymes play a crucial role in various biological processes, including defense mechanisms and lignin degradation in fungi. The extraction process was meticulously optimized to maximize enzyme yield while maintaining enzymatic activity. Initial extraction involved mechanical disruption and homogenization of mushroom tissue, followed by enzymatic release through the use of appropriate buffer solutions. The extracted crude enzyme solution was subjected to purification using techniques such as ammonium sulfate precipitation, ion exchange chromatography, and size exclusion chromatography. The purification steps aimed to achieve high specificity and activity of the peroxidase enzyme. Throughout the extraction and purification process, various parameters were monitored and controlled, including pH, temperature, and salt concentration, to ensure optimal enzyme stability and functionality. Enzyme activity was assayed using standard colorimetric methods, and the purified peroxidase enzyme's characteristics were analyzed in terms of substrate specificity, pH and temperature optima, and kinetic parameters. This study provides insights into the efficient extraction and purification of peroxidase from Pleurotus tuberregium, contributing to the understanding of enzyme isolation techniques and their potential applications in biotechnology, including wastewater treatment, biosensors, and pharmaceuticals. The results underscore the significance of optimizing extraction and purification protocols for achieving high yields of active peroxidase enzymes, thereby enhancing their usability in various industrial and research settings.