Antifungal properties of haem peroxidase from Acorus calamus.

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 d

SUBMITTER: Ghosh M 

PROVIDER: S-EPMC2803583 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature