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A basic peroxidase from wheat kernel with antifungal activity.

C Caruso·G Chilosi·L Leonardi·L Bertini·P Magro·V Buonocore·C Caporale
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Abstract

A basic heme-peroxidase (WP1) was purified to homogeneity from wheat (Triticum aestivum) kernels. The protein was not glycosylated and exhibited a molecular mass of 36 kDa and a pI of 8.0. The N-terminal amino acid sequence revealed a very high similarity with a wheat flour peroxidase allergen associated with baker's asthma. WPI showed indole-3-acetic acid oxidase activity in the presence of Mn2+ and phenolic cofactors. Antifungal assays performed in vitro towards phytopathogenic fungi indicated that WP1 was active in inhibiting germ tube elongation. This first report on antifungal properties of a heme-peroxidase gives experimental support to the idea that peroxidases play a defensive role against invading pathogens.

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Amino Acid SequenceAntifungal AgentsBotrytisFusariumManganeseMolecular Sequence DataPeroxidasePeroxidasesSeedsSequence HomologyTrichodermaTriticumJournal ArticleResearch Support, Non-U.S. Gov't

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C Caruso, G Chilosi, L Leonardi, L Bertini, P Magro, V Buonocore, C Caporale. 2001. A basic peroxidase from wheat kernel with antifungal activity.. https://doi.org/10.1016/s0031-9422(01)00226-6

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