Characterization of a novel antifungal protein produced by Paenibacillus polymyxa isolated from the wheat rhizosphere
| Autor: | Baocheng Xu, Lingxia Jiao, Zhao Ruixiang, Li Pan, Mingming Zhu, Junjian Ran, Jianrong Shi |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Fusarium
030309 nutrition & dietetics Microbiology law.invention 03 medical and health sciences chemistry.chemical_compound 0404 agricultural biotechnology law medicine Glycosyl Soil Microbiology Triticum Plant Diseases 0303 health sciences Rhizosphere Nutrition and Dietetics biology Chemistry food and beverages 04 agricultural and veterinary sciences Trypsin biology.organism_classification Proteinase K 040401 food science Fungicides Industrial biology.protein Recombinant DNA Paenibacillus polymyxa Agronomy and Crop Science Bacteria Food Science Biotechnology medicine.drug |
| Zdroj: | Journal of the Science of Food and Agriculture. 101:1901-1909 |
| ISSN: | 1097-0010 0022-5142 |
| Popis: | Background Fusarium head blight (FHB) is one of the disasters that seriously harm wheat and other small grain crops. It causes spoilage and mildew of the grain leading to a significant decline in the yield and quality of the grain. This research aimed to isolate antagonistic bacteria to purify antifungal proteins. A strain was isolated from the rhizosphere of healthy wheat in a wheat field affected by a severe FHB epidemic. This isolated strain was tentatively identified as Paenibacillus polymyxa 7F1, which displayed a strong inhibitory effect against several other pathogens. One novel antifungal protein was purified from the P. polymyxa 7F1 and successfully expressed. Results A crude culture of P. polymyxa 7F1 demonstrated antifungal activity that was stable at a temperature range of 60-90 °C and a pH range of 2.6-9.0. However, the antifungal activity of the P. polymyxa 7F1 was inhibited with proteinase K, trypsin, and neutral protease treatment. A 36 kDa protein with broad-spectrum antifungal activity was purified from the P. polymyxa 7F1. A glycosyl hydrolase domain was identified from this protein through liquid chromatography-mass spectrometry (LC-MS) analysis. A recombinant plasmid pET32a(+)/36kd for prokaryotic expression was constructed, and the renatured p36kd protein demonstrated similar antifungal activity to the 36 kDa protein purified from the P. polymyxa 7F1. Conclusion A novel antifungal protein produced by P. polymyxa 7F1 was purified and expressed. The recombinant protein showed good antifungal activity as the novel purified protein. The novel antifungal protein provides an effective way to control the Fusarium head blight. © 2020 Society of Chemical Industry. |
| Databáze: | OpenAIRE |
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