Fengycin C produced by Bacillus subtilis EA-CB0015

Bacillus subtilis EA-CB0015 was isolated from the phyllosphere of a banana plant and tested for its potential to produce bioactive compounds against Mycosphaerella fijiensis -- Using a dual plate culture technique the cell-free supernatant of B. subtilis EA-CB0015 produced inhibition values of 89 ±...

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Autores:
Ceballos, Isabel
J. Mira, John
Argel, Luz Edith
Orduz Peralta, Sergio
Romero Tabarez, Magally
Villegas Escobar, Valeska
Tipo de recurso:
Fecha de publicación:
2014
Institución:
Universidad EAFIT
Repositorio:
Repositorio EAFIT
Idioma:
eng
OAI Identifier:
oai:repository.eafit.edu.co:10784/7258
Acceso en línea:
http://hdl.handle.net/10784/7258
Palabra clave:
BACILLUS SUBTILIS
COMPUESTOS BIOACTIVOS
ESPECTROMETRÍA DE MASAS
AMINOÁCIDOS
HONGOS FITOPATÓGENOS
COMPUESTOS ORGANOCÍCLICOS
LACTONAS
Bacillus subtilis
Bioactive compounds
Mass spectrometry
Amino acids
Phytopathogenic fungi
Organic cyclic compounds
Lactones
Tirosina
Fengycin
Rights
License
Copyright © 2013 The American Chemical Society and American Society of Pharmacognosy
Description
Summary:Bacillus subtilis EA-CB0015 was isolated from the phyllosphere of a banana plant and tested for its potential to produce bioactive compounds against Mycosphaerella fijiensis -- Using a dual plate culture technique the cell-free supernatant of B. subtilis EA-CB0015 produced inhibition values of 89 ± 1% -- The active compounds were purified by solid-phase extraction and HPLC, and their primary structures determined using mass spectrometry and amino acid analysis -- A new fengycin isoform, fengycin C, with the amino acid sequence Glu-Orn-Tyr-Thr-Glu-Val-Pro-Gln-Thr-Ile was isolated -- The peptidic moiety differs from fengycin B at position 9 and from fengycin A at positions 6 and 9 -- The β-hydroxy fatty acyl chain is connected to the N-terminal of the decapeptide and can be saturated or unsaturated, ranging from 14 to 18 carbons -- The C-terminal residue of the peptidic moiety is linked to the tyrosine residue at position 3, forming the branching point of the acyl peptide and the eight-membered cyclic lactone