Lipopeptides and their analogues are of increasing interest due to their amphiphilic structures and potential applications in various fields. Three purified lipopeptides analogues were obtained at the same time after two-step column-chromatographic purification from cell-free broth cultivated by Bac
Isolation and characterization of a C12-lipopeptide produced by Bacillus subtilis HSO 121
β Scribed by Xiang-Yang Liu; Shi-Zhong Yang; Bo-Zhong Mu
- Publisher
- John Wiley and Sons
- Year
- 2008
- Tongue
- English
- Weight
- 711 KB
- Volume
- 14
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.1017
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β¦ Synopsis
Abstract
A new lipopeptide with C~12~ fatty acid has been isolated from the cell broth of Bacillus subtilis HSO121 by chromatographic methods, which is believed to be the homologue of lipopeptides. The fatty acid portion was methylated and analyzed by GC/MS, ESI QβTOF MS and ^1^HβNMR. The peptide portion, of which the amino acid composition was obtained by HPLC combined with a phenyl isothiocyanate (PITC) derivatization methods, was analyzed by ESI QβTOF MS. Comparing the obtained results with surfactin C~13~ showed that the new lipopeptide has a peptide moiety similar to that of surfactin and the difference exists in the fatty acid portion, which is an isoβC~12~Ξ²βhydroxy fatty acid. The critical micelle concentration (CMC) of this new homologue is estimated to be 6.27 Γ 10^β5^ mol/l in 10 mmol/l phosphate buffer solution (PBS, pH 8.0) at 30 Β°C, and the surface tension at CMC (Ξ³~CMC~) achieved is as little as 27.71 mN/m. The hemolytic activities of the C~12~βlipopeptide on 2% human erythrocytes showed a HC~50~ of 26.5 Β΅mol/l. Copyright Β© 2008 European Peptide Society and John Wiley & Sons, Ltd.
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