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

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

School of Biological Science and Bioengineering, South China University of Technology, Guangzhou 510006, China
Author to whom correspondence should be addressed.
Received: 1 June 2012 / Revised: 10 June 2012 / Accepted: 11 June 2012 / Published: 14 June 2012
(This article belongs to the Section Natural Products)
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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 (CC BY 3.0).

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MDPI and ACS Style

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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