Antifungal properties of haem peroxidase from Acorus calamus

75Citations
Citations of this article
65Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

• Background and Aims: Plants have evolved a number of inducible defence mechanisms against pathogen attack, including synthesis of pathogenesis-related proteins. The aim of the study was to purify and characterize antifungal protein from leaves of Acorus calamus. • Methods: Leaf proteins from A. calamus were fractionated by cation exchange chromatography and gel filtration and the fraction inhibiting the hyphal extension of phytopathogens was characterized. The temperature stability and pH optima of the protein were determined and its presence was localized in the leaf tissues. • Key Results: The purified protein was identified as a class III haem peroxidase with a molecular weight of approx. 32 kDa and pI of 7.93. The temperature stability of the enzyme was observed from 5°C to 60°C with a temperature optimum of 36°C. Maximum enzyme activity was registered at pH 5.5. The pH and temperature optima were corroborated with the antifungal activity of the enzyme. The enzyme was localized in the leaf epidermal cells and lumen tissues of xylem, characteristic of class III peroxidases. The toxic nature of the enzyme which inhibited hyphal growth was demonstrated against phytopathogens such as Macrophomina phaseolina, Fusarium moniliforme and Trichosporium vesiculosum. Microscopic observations revealed distortion in the hyphal structure with stunted growth, increased volume and extensive hyphal branching. • Conclusions: This study indicates that peroxidases may have a role to play in host defence by inhibiting the hyphal extension of invading pathogens. © The Author 2006. Published by Oxford University Press on behalf of the Annals of Botany Company. All rights reserved.

Cite

CITATION STYLE

APA

Ghosh, M. (2006). Antifungal properties of haem peroxidase from Acorus calamus. Annals of Botany, 98(6), 1145–1153. https://doi.org/10.1093/aob/mcl205

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free