Structural Analysis of the Lipopeptide Produced by the Bacillus subtilis Mutant R2-104 with Mutagenesis.
Appl Biochem Biotechnol
; 179(6): 973-85, 2016 Jul.
Article
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| MEDLINE
| ID: mdl-27020566
ABSTRACT
The lipopeptide and its homologues are a kind of the five major biosurfactants with prominent interfacial and biological activities. A suite of mutagenesis method was adopted to expose a wild lipopeptide-producing strain Bacillus subtilis HSO121 to improve lipopeptide yield, and a stable mutant named R2-104 with a 2.0-fold production of lipopeptide was obtained. Compared to that of the wild strain HSO121, the lipopeptide produced by R2-104 showed a similar surface activity, but the course profiles of lipopeptide production during cultivation were different, with the peak yield of 500 mg at about 9 h by R2-104, and 400 mg at about 5 h by HSO121. The constituent abundance of the lipopeptide homologues produced by R2-104 was also different from that by HSO121. Combined methods of ESI-MS, GC-MS and MS-MS were applied for structural characterization of lipopeptide homologues, and it showed that the lipopeptides produced by R2-104 and HSO121 were attributed to a surfactin family with different constituents. The dominant constituent of the surfactin family produced by R2-104 was anteiso C15-surfactin with a relative content of 43.8 %, while the dominant one produced by HSO121was iso C14-surfactin with a relative content of 33.1 %.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Tensoactivos
/
Bacillus subtilis
/
Proteínas Mutantes
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Lipopéptidos
Idioma:
En
Revista:
Appl Biochem Biotechnol
Año:
2016
Tipo del documento:
Article