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Abstract

PURIFICATION AND CHARACTERIZATION OF PEROXIDASE FORM PHYLLANTHUS AMARUS LEAVES

Paras Jain*, H. P. Sharma, Sandya Rai and Vishal Ahuja

ABSTRACT

Peroxidase is an iron enzyme that catalyzes many oxidation reduction reactions using hydrogen peroxide as electron acceptor. It is universally present in bacteria, fungi, plants and animals. Plant peroxidase belongs toclass III which mainly contribute to removal of hydrogen peroxide from cell organelles; oxidation of toxins; biosynthesis of the cell wall and defense against wound. Apart from cellular function, peroxidase can be used for treatment of industrial wastes specially for removal and detoxification of phenols from effluent. Manufacturing of adhesives, computer chips and car parts are some other industrial applications of peroxidases. The present work was designed to extract peroxidase from plant source. Different parts of Phyllantus amarus was screened for peroxidase using optimized buffer and pH. Extracted enzyme was purified using ammonium sulfate and immobilized on calcium alginate beads.Crude enzyme extracted from sample was 84.52 U/mg of protein which increases to 148.09 U/ml after purification. Optimization of purification process exhibited increase in enzyme recovery. Further enzyme immobilized on calcium alginate. Immobilized enzyme showed remarkable stability and reusability with after immobilization which suggested the suture applicability.

Keywords: Oxidoreductase, peroxidase, immobilization, wound healing


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