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An antifungal protein produced by <em>Bacillus licheniformis</em> 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 <em>Aspergillus niger</em>, <em>Magnaporthe oryzae</em> and<em> </em><em>Rhizoctonia solani</em>. 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 <em>Rhizoctonia solani</em> as the indicator strain, the EC<sub>50</sub> 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,<em> M. lysodeikticus</em>, and <em>p</em>-nitrophenyl-<em>N</em>-acetylglucosaminide.