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Purification and partial characterization of a thermostable antimicrobial protein from Bacillus subtilis FB123.
- Source :
-
World Journal of Microbiology & Biotechnology . Aug2015, Vol. 31 Issue 8, p1285-1290. 6p. - Publication Year :
- 2015
-
Abstract
- Antimicrobial proteins/peptides have attracted much attention because of their potential use in the industrial setting. In the present study, a thermostable antimicrobial protein (BSAMP) was purified from the culture supernatant of Bacillus subtilis FB123 by ammonium sulfate precipitation, gel chromatography on Sephacryl S-200 High Resolution, and ion exchange chromatography on DEAE Sepharose Fast Flow column. The molecular weight of the purified BSAMP was 54 kDa, as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis both in the absence and presence of β-mercaptoethanol. Its isoelectric point was determined to be 5.24 by isoelectric focusing electrophoresis. Periodic acid-Schiff staining revealed BSAMP to be a glycoprotein. Maximum activity was obtained at pH 6.0, with over 79 % maximum activity retained at pH 3.0-5.0 and pH 7.0-9.0, respectively. BSAMP was shown to be highly thermostable, as its activity did not change obviously after treatment at 100 °C. However, it was partially sensitive to papain, trypsin, and alkali proteases. Finally, the bacterial protein exhibited broad-spectrum antimicrobial activity against several pathogenic organisms. These findings suggested that BSAMP should be further developed as a natural antibacterial agent for disease prevention in aquiculture and agriculture. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09593993
- Volume :
- 31
- Issue :
- 8
- Database :
- Academic Search Index
- Journal :
- World Journal of Microbiology & Biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 103547038
- Full Text :
- https://doi.org/10.1007/s11274-015-1871-9