枯草芽孢杆菌SL-13的生防性能及其抗菌几丁质酶特性研究(英文)

来源 :Chinese Journal of Chemical Engineering | 被引量 : 0次 | 上传用户:koel
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The seed germination and tomato seedling tests showed that Bacillus subtilis SL-13 could promote the sprouting and seedling growth of tomato.The fresh and dry weight of tomato seedlings increased 42.86%and 18.75%,respectively.The control efficacies of the SL-13 to tomato Rhizoctonia rot were 20.65%and 35.23%in the greenhouse and field,respectively.The growth of the plant-pathogenic fungus Rhizoctonia solani was considerably inhibited in the presence of the strain SL-13 culture supernatant.The main antifungal protein was detected to be chitinase through vitro assay.The chitinase was purified with DEAE-Sepharose fast flow ion exchange column chromatography and Sephadex G-75 gel filtration for further characterization.The optimal pH and temperature for the chitinase activity were 7.0 and 50°C,respectively.It was demonstrated that the enzyme was stable at pH 5-9 and 40-60°C.70%of the enzyme activity was retained when incubated at 121°C and 0.11 MPa for 20 min,and the enzyme was not sensitive to protease K and ultraviolet radiation.Thus it is suitable for effective biological control in relatively unstable environment. The seed germination and tomato seedling tests showed that Bacillus subtilis SL-13 could promote the sprouting and seedling growth of tomato. The fresh and dry weight of tomato seedlings increased 42.86% and 18.75%, respectively. The control efficacies of the SL-13 to tomato Rhizoctonia rot were 20.65% and 35.23% in the greenhouse and field, respectively. The growth of the plant-pathogenic fungus Rhizoctonia solani was root inhibited in the presence of the strain SL-13 culture supernatant. The main antifungal protein was detected to be chitinase through vitro assay. The chitinase was purified with DEAE-Sepharose fast flow ion exchange column chromatography and Sephadex G-75 gel filtration for further characterization. The optimal pH and temperature for the chitinase activity were 7.0 and 50 ° C, respectively. It was demonstrated that the enzyme was stable at pH 5-9 and 40-60 ° C. 70% of the enzyme activity was retained when incubated at 121 ° C and 0.11 MPa for 20 min, and the enzyme was not sens itive to protease K and ultraviolet radiation. It is suitable for effective biological control in relatively unstable environment.
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