Enzymatic Characterisation of Lignin Peroxidase from Luffa aegyptiaca Fruit Juice

Abstract

Luffa aegyptiaca fruit has been assayed for the presence of lignin peroxidase activity using veratryl alcohol as the substrate. The fruit juice contained activity of 3.14 U/ml which was much higher than 0.075 U/ml reported in the culture filtrate of Phanarochaete chrysosporium ATCC-24725. The Km value of the lignin peroxidase using veratryl alcohol as the variable substrate in 50mM phosphate buffer pH 2.5 at 25&degC was found to be 50 μM respectively. The pH and temperature optima of the lignin peroxidase were 2.4 and 22&degC, respectively. The present article reports viable method to explore rich sources of lignin peroxidase from plants which can be used as a mediator in oxidative organic transformations within green chemistry domain ensuring ecofriendly synthesis of bioorganic molecules of pharmaceutical value.