Beschreibung:
<jats:p>A cytosolic protein was purified from<jats:italic>Escherichia coli</jats:italic>BL21 that demonstrated potent antifungal activity against pathogenic strains of<jats:italic>Aspergillus fumigatus</jats:italic>,<jats:italic>Aspergillus flavus</jats:italic>,<jats:italic>Aspergillus niger</jats:italic>and<jats:italic>Candida albicans</jats:italic>. The MIC of purified protein from<jats:italic>E. coli</jats:italic>BL21 (PPEBL21) against<jats:italic>Aspergillus</jats:italic>species and<jats:italic>C. albicans</jats:italic>was 1.95–3.98 and 15.62 μg ml<jats:sup>−1</jats:sup>, respectively.<jats:italic>In vitro</jats:italic>toxicity tests demonstrated no cytotoxicity of PPEBL21 to human erythrocytes up to the tested concentrations of 1250 μg ml<jats:sup>−1</jats:sup>. Amphotericin B was lethal to 100 % of human erythrocytes at a concentration of 37.5 μg ml<jats:sup>−1</jats:sup>. The N-terminal amino acid sequence of PPEBL21 was found to be DLAEVASR, which showed 75 % sequence similarity with alcohol dehydrogenase of yeast. Mass fingerprinting by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry also substantiated these observations. The results suggested that<jats:italic>E. coli</jats:italic>BL21 might be an important bioresource of lead molecules for developing new peptide-based therapies for treating fungal infections.</jats:p>