Keywords: Bacopa monnieri, oxidoreductase, peroxidase, immobilization, wound healing
Peroxidase is an oxidoreductase enzyme catalysing many oxidation reduction reactions in presence of iron as cofactor. Main function of peroxidase is the scavenging of reactive oxygen species to reduce oxidative stress and damage. It is universally present in living organisms such as bacteria, fungi, plants and animals. Peroxidases also contribute in lignin biosynthesis, hormone generation, and detoxification by removal of hydrogen peroxide from cell organelles and oxidation of toxins. Industrially, peroxidases are also important for the removal of phenols from industrial wastes, manufacturing of adhesives, and computer chips. On the other hand Bacopa monnieri is one of the well known plants with immense importance since ages. The present work included both the enzyme and plant resource as peroxidase enzyme was extract from Bacopa monnieri. After screening different parts of Bacopa monnieri fresh leaves were used for partial purification peroxidases enzyme. Crude enzyme extracted from sample was partially purified by using ammonium sulfate precipitation which was further used for immobilization. As result of purification peroxidase activity was enhanced from 63.51 U/mg of protein to 123.87U/mg. Optimization of purification process exhibited increase in enzyme recovery. Moreover immobilized enzyme also showed remarkable stability and reusability with after immobilization which suggested the suture applicability.