کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2007472 | 1066376 | 2008 | 7 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: First isolation of a novel thermostable antifungal peptide secreted by Aspergillus clavatus First isolation of a novel thermostable antifungal peptide secreted by Aspergillus clavatus](/preview/png/2007472.png)
A novel antifungal peptide produced by an indigenous fungal strain (VR) of Aspergillus clavatus was purified. The antifungal peptide was enriched in the supernatant after heat treatment at 70 °C. The thermostable character was exploited in the first purification step, as purified peptide was obtained after ultrafiltration and reverse phase-HPLC on C18 column application. The purified peptide named “AcAFP” for A. clavatus antifungal peptide, has molecular mass of 5773 Da determined by MALDI-ToF spectrometry. The N-terminal sequence showed a notable identity to the limited family of antifungal peptides produced by ascomycetes fungi. The AcAFP activity remains intact even after heat treatment at 100 °C for 1 h confirming its thermostability. It exhibits a strong inhibitory activity against mycelial growth of several serious human and plant pathogenic fungi: Fusariuym oxysporum, Fusarium solani, Aspergillus niger, Botrytis cinerea, Alternaria solani, whereas AcAFP did not affect yeast and bacterial growth.
Journal: Peptides - Volume 29, Issue 11, November 2008, Pages 1871–1877