ArticleWorld journal of microbiology & biotechnology2016
Purification and characterization of a potential antifungal protein from Bacillus subtilis E1R-J against Valsa mali.
Article in World journal of microbiology & biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 37 citations in OpenAlex.
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- The antimicrobial activity of protein elicitor AMEP412 against Streptomyces scabiei.World journal of microbiology & biotechnology · 2020Article
- Study on the optimal antagonistic effect of a bacterial complex againstOpen life sciences · 2020Article
- Antifungal Mechanism of Dipicolinic Acid and Its Efficacy for the Biocontrol of Pear Valsa Canker.Frontiers in microbiology · 2020Article
- Purification and identification of a novel antifungal protein from Bacillus subtilis XB-1.World journal of microbiology & biotechnology · 2019Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
In order to identify the antagonistic substances produced by Bacillus subtilis E1R-J as candidate of biocontrol agents for controlling Apple Valsa Canker, hydrochloric acid precipitation, reverse phase chromatography, gel filtration, and ion exchange chromatography were used. The purified fraction EP-2 showed a single band in native-polyacrylamide gel electrophoresis (native-PAGE) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Fraction EP-2 was eluted from native-PAGE and showed a clear inhibition zone against V. mali 03-8. These results prove that EP-2 is one of the most important antifungal substances produced by B. subtilis E1R-J in fermentation broth. SDS-PAGE and Nano-LC-ESI-MS/MS analysis results demonstrated that EP-2 was likely an antifungal peptide (trA0A086WXP9), with a relative molecular mass of 12.44 kDa and isoelectric point of 9.94. The examination of antagonistic mechanism under SEM and TEM showed that EP-2 appeared to inhibit Valsa mali 03-8 by causing hyphal swelling, distortion, abnormality and protoplasts extravasation. Inhibition spectrum results showed that antifungal protein EP-2 had significantly inhibition on sixteen kinds of plant pathogenic fungi. The stability test results showed that protein EP-2 was stable with antifungal activity at temperatures as high as 100 °C for 30 min and in pH values ranging from 1.0 to 8.0, or incubated with each 5 mM Cu(2+), Zn(2+), Mg(2+), or K(+). However, the antifungal activity was negatively affected by Proteinase K treatment.
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