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Molecules 2012, 17(6), 7336-7347; doi:10.3390/molecules17067336
Article

Isolation and Partial Characterization of an Antifungal Protein Produced by Bacillus licheniformis BS-3

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Received: 1 June 2012 / Revised: 10 June 2012 / Accepted: 11 June 2012 / Published: 14 June 2012
(This article belongs to the Section Metabolites)
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Abstract

An 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.
Keywords: Bacillus licheniformis; antifungal protein; chromatography isolation; proteinase Bacillus licheniformis; antifungal protein; chromatography isolation; proteinase
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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.

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