Factors affecting production and stability of the AcAFP antifungal peptide secreted by Aspergillus clavatus.
We have previously reported the identification of a small, basic and cysteine-rich antifungal peptide (AcAFP) secreted by Aspergillus clavatus and shown its ability to prevent growth of various human- and plant-pathogenic filamentous fungi. In this study, we sought to determine the physiological/microbiological requirements to enhance the AcAFP production and the conditions influencing its stability. The maximum of AcAFP production was obtained when A. clavatus was grown on 2% glycerol as sole carbon source and 100 mM NaCl. The AcAFP expression was shown to be influenced by pH, being suppressed under acidic (pH 5) and strongly induced under alkaline conditions. The activity of the purified AcAFP was not affected by temperature; it loosed approximately 20% of its activity after 3 h at 100 degrees C and was efficient through a large pH range (pH 5-12) with an optimum at pH 8. AcAFP activity decreased at high ionic strength and in the presence of 10 mM of divalent cations (Mn2+, Fe2+ and Ca2+).
Skouri-Gargouri
Houda
H
Laboratoire de Génétique Moléculaire des Eucaryotes, Centre de Biotechnologie de Sfax, Sfax, Tunisia.
Jellouli-Chaker
Neila
N
Gargouri
Ali
A
D000935:Antifungal Agents / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D001230:Aspergillus / Q000378:metabolism*; D002413:Cations, Divalent / Q000494:pharmacology; D003470:Culture Media / Q000737:chemistry; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005656:Fungal Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000494:pharmacology; D005670:Fusarium / Q000187:drug effects; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008826:Microbial Sensitivity Tests; D009994:Osmolar Concentration; D055550:Protein Stability
C539765:AFP peptide, Aspergillus clavatus; D000935:Antifungal Agents; D002413:Cations, Divalent; D003470:Culture Media; D004791:Enzyme Inhibitors; D005656:Fungal Proteins