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Isolation and Partial Characterization of an Antifungal Protein Produced by Bacillus licheniformis BS-3
AbstractAn antifungal protein produced by Bacillus licheniformis strain BS-3 was purified to homogeneity by ammonium sulfate precipitation, DEAE-52 column chromatography and Sephadex G-75 column chromatography. The purified protein was designated as F2 protein, inhibited the growth of Aspergillus niger, Magnaporthe oryzae and Rhizoctonia solani. F2 protein was a monomer with approximately molecular weight of 31 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gave a single peak on High Performance Liquid Chromatography (HPLC). Using Rhizoctonia solani as the indicator strain, the EC50 of F2 protein was 35.82 µg/mL, displaying a higher antifungal activity in a range of pH 6.0 to pH 10.0, and at a temperature below 70 °C for 30 min. F2 protein was moderately resistant to hydrolysis by trypsin, proteinase K, after which its relative activities were 41.7% and 59.5%, respectively. F2 protein was assayed using various substrates to determine the enzymatic activities, the results showed the hydrolyzing activity on casein, however, no enzymatic activities on colloidal chitin, CM-cellulose, xylan, M. lysodeikticus, and p-nitrophenyl-N-acetylglucosaminide.
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Cui, T.-B.; Chai, H.-Y.; Jiang, L.-X. Isolation and Partial Characterization of an Antifungal Protein Produced by Bacillus licheniformis BS-3. Molecules 2012, 17, 7336-7347.View more citation formats
Cui T-B, Chai H-Y, Jiang L-X. Isolation and Partial Characterization of an Antifungal Protein Produced by Bacillus licheniformis BS-3. Molecules. 2012; 17(6):7336-7347.Chicago/Turabian Style
Cui, Tang-Bing; Chai, Hai-Yun; Jiang, Li-Xiang. 2012. "Isolation and Partial Characterization of an Antifungal Protein Produced by Bacillus licheniformis BS-3." Molecules 17, no. 6: 7336-7347.
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