Enzymatic Characterisation of Lignin Peroxidase from <i>Luffa aegyptiaca</i> 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 K m 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.