Fengycin C produced by Bacillus subtilis EA-CB0015.

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dc.citation.journalTitleJOURNAL OF NATURAL PRODUCTSspa
dc.contributor.authorVillegas-Escobar, Valeska
dc.contributor.authorCeballos, Isabel
dc.contributor.authorMira, John J.
dc.contributor.authorEdith Argel, Luz
dc.contributor.authorOrduz Peralta, Sergio
dc.contributor.authorRomero-Tabarez, Magally
dc.contributor.departmentUniversidad EAFIT. Departamento de Cienciasspa
dc.contributor.researchgroupCiencias Biológicas y Bioprocesos (CIBIOP)spa
dc.date.accessioned2021-03-23T20:08:54Z
dc.date.available2021-03-23T20:08:54Z
dc.date.issued2013-04-26
dc.description.abstractBacillus 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 beta-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.eng
dc.identifierhttps://eafit.fundanetsuite.com/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=1313
dc.identifier.doi10.1021/np300574vspa
dc.identifier.issn01633864spa
dc.identifier.issn15206025spa
dc.identifier.otherWOS;000355215900006
dc.identifier.otherSCOPUS;2-s2.0-84929657569
dc.identifier.urihttp://hdl.handle.net/10784/26790
dc.language.isoengeng
dc.publisherAMER CHEMICAL SOC
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84876897092&doi=10.1021%2fnp300574v&partnerID=40&md5=3b60a281b90e9967e2978b4f1653412e
dc.rightshttps://v2.sherpa.ac.uk/id/publication/issn/0163-3864
dc.sourceJOURNAL OF NATURAL PRODUCTS
dc.subject.keywordamino acideng
dc.subject.keywordantifungal agenteng
dc.subject.keywordfengycin ceng
dc.subject.keywordnatural producteng
dc.subject.keywordtyrosineeng
dc.subject.keywordunclassified drugeng
dc.subject.keywordarticleeng
dc.subject.keywordBacillus subtiliseng
dc.subject.keywordbacterial straineng
dc.subject.keywordbacterium isolationeng
dc.subject.keywordbiological activityeng
dc.subject.keywordcarboxy terminal sequenceeng
dc.subject.keywordcell free systemeng
dc.subject.keywordculture techniqueeng
dc.subject.keyworddrug structureeng
dc.subject.keyworddrug synthesiseng
dc.subject.keywordfunguseng
dc.subject.keywordhigh performance liquid chromatographyeng
dc.subject.keywordmass spectrometryeng
dc.subject.keywordMycosphaerella fijiensiseng
dc.subject.keywordnonhumaneng
dc.subject.keywordnucleotide sequenceeng
dc.subject.keywordsolid phase extractioneng
dc.subject.keywordAmino Acid Sequenceeng
dc.subject.keywordAntifungal Agentseng
dc.subject.keywordAscomycotaeng
dc.subject.keywordBacillus subtiliseng
dc.subject.keywordLipopeptideseng
dc.subject.keywordMicrobial Sensitivity Testseng
dc.subject.keywordMolecular Structureeng
dc.subject.keywordMusaeng
dc.subject.keywordPeptideseng
dc.subject.keywordCycliceng
dc.subject.keywordProtein Isoformseng
dc.subject.keywordTyrosineeng
dc.subject.keywordBacillus subtiliseng
dc.subject.keywordMycosphaerella fijiensiseng
dc.titleFengycin C produced by Bacillus subtilis EA-CB0015.eng
dc.typearticleeng
dc.typeinfo:eu-repo/semantics/articleeng
dc.typeinfo:eu-repo/semantics/publishedVersioneng
dc.typepublishedVersioneng
dc.type.localArtículo

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