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Renganathan, V. and Gold, M.H. (1986) Spectral Characterization of the Oxidized States of Lignin Peroxidase, an Extracellular Heme Enzyme from the White Rot Basidiomycete Phanerochaete chrysosporium. Biochemistry, 25, 1626-1631.
http://dx.doi.org/10.1021/bi00355a027

has been cited by the following article:

• TITLE: Enzymatic Characterisation of Lignin Peroxidase from Luffa aegyptiaca Fruit Juice

  AUTHORS: Nivedita Rai, Meera Yadav, Hardeo Singh Yadav

  KEYWORDS: Lignin Peroxidase, Metalloenzyme, Heme, Biomass, Bioconversion, Luffa aegyptiaca

  JOURNAL NAME: American Journal of Plant Sciences, Vol.7 No.3, March 29, 2016

  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°C was found to be 50 μM respectively. The pH and temperature optima of the lignin peroxidase were 2.4 and 22°C, 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.