Purification of peroxidase from the medicinal herb Andrographis paniculata causing fungal hyphal distortion



Peroxidases are ubiquitous in plants and their pattern of expression depends on tissue, development stage and environmental stimuli. They are involved in numerous physiological functions, including defense against pathogens and insect pests. The present study was conducted to isolate and purify a constitutive leaf peroxidase from the medicinal herb, Andrographis paniculata. The enzyme was purified through a series of purification steps and a 35kDa peroxidase was purified to homogeneity with pI value of 6.0. In vitro hyphal extension inhibition assay against the forest pathogen Trichosporium vesiculosum revealed significant morphological distortion of the protein treated hyphae. Key words: antifungal protein, defense, hyphal inhibition, oxido reductases, pathogenesis-related protein
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