Purification and partial characterization of a bacteriocin produced by Eikenella corrodens.
J Appl Microbiol
; 104(2): 508-14, 2008 Feb.
Article
em En
| MEDLINE
| ID: mdl-17922820
AIMS: The purpose of this study was to purify and characterize a bacteriocin produced by Eikenella corrodens A32E2. METHODS AND RESULTS: Peptostreptococcus anaerobius ATCC27337 was used as indicator strain in antagonistic assays for bacteriocin-producing E. corrodens A32E2. Protein extraction was influenced by pH and buffer composition. The protein was active in the pH range 6-8. Inhibitory activity was lost by both heating and treatment with proteolytic enzymes and decreased with organic solvents. The substance is rather unstable but maintains 100% of its activity after being exposed to acetone and when stored at -70 degrees C. The antagonistic substance was first precipitated by ammonium sulfate and further partially purified by Mono-Q FPLC and C-18 HPLC. Mass spectrometry analysis showed that the molecular mass was 23 625 Da, and the sequence obtained for the N-terminus was: Met-Asn-Phe-Asp-Glu-Lys-Val-Gly-Lys-Val-X-Phe-Lys-Val-Gly-Asp. CONCLUSIONS: The evidence presented in this study supports the idea that an antagonistic substance produced by E. corrodens A32E2 isolated from a periodontal diseased site is a novel bacteriocin, which we designate corrodecin. SIGNIFICANCE AND IMPACT OF THE STUDY: We anticipated that corrodecin might play an important role at the periodontal site. This compound could also be attractive in biotechnological applications as an interesting tool for oral ecosystem control.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Bacteriocinas
/
Eikenella corrodens
Limite:
Humans
Idioma:
En
Revista:
J Appl Microbiol
Assunto da revista:
MICROBIOLOGIA
Ano de publicação:
2008
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Reino Unido