| Literature DB >> 23461648 |
Valeska Villegas-Escobar1, Isabel Ceballos, John J Mira, Luz Edith Argel, Sergio Orduz Peralta, Magally Romero-Tabarez.
Abstract
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.Entities:
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Year: 2013 PMID: 23461648 DOI: 10.1021/np300574v
Source DB: PubMed Journal: J Nat Prod ISSN: 0163-3864 Impact factor: 4.050