%0 Journal Article
%T Isolation and Partial Characterization of an Antifungal Protein Produced by Bacillus licheniformis BS-3
%A Tang-Bing Cui
%A Hai-Yun Chai
%A Li-Xiang Jiang
%J Molecules
%D 2012
%I MDPI AG
%R 10.3390/molecules17067336
%X 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 ¦Ìg/mL, displaying a higher antifungal activity in a range of pH 6.0 to pH 10.0, and at a temperature below 70 ¡ãC 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.
%K Bacillus licheniformis
%K antifungal protein
%K chromatography isolation
%K proteinase
%U http://www.mdpi.com/1420-3049/17/6/7336