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Keywords:

  • Croton tiglium;
  • bioactive peptide/protein;
  • antibacterial;
  • antifungal

Abstract

This study describes the activity-guided isolation and purification of a novel antimicrobial protein from the seed of Croton tiglium Linn. Purification was carried out by (NH4)2SO4 precipitation, gel filtration and DEAE-cellulose ion-exchange chromatography. Antifungal and antibacterial activities were determined after each purification step. SDS-polyacrylamide gel electrophoresis revealed that the purified protein was a monomer with molecular mass of 50 kDa. This is a first report on purification of a protein from Croton tiglium, which possesses a strong and broad spectrum antimicrobial activity. Copyright © 2008 John Wiley & Sons, Ltd.