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dc.creatorDimitrijević, Rajna
dc.creatorStojanović, Marijana
dc.creatorŽivković, Irena
dc.creatorPetersen, Arnd
dc.creatorJankov, Ratko
dc.creatorDimitrijević, Ljiljana
dc.creatorGavrović-Jankulović, Marija
dc.date.accessioned2021-02-18T10:33:44Z
dc.date.available2021-02-18T10:33:44Z
dc.date.issued2009
dc.identifier.issn1364-5072
dc.identifier.urihttp://intor.torlakinstitut.com/handle/123456789/275
dc.description.abstractAims: This study focuses on the isolation and characterization of a peptide with bacteriocin-like properties isolated from Lactobacillus rhamnosus strain 68, previously identified by 16S rRNA gene sequencing and originating from human gastrointestinal flora. Methods and Results: The peptide was isolated from a supernatant of bacteria maintained under restrictive conditions by a combination of ethanol precipitation and reversed-phase chromatography. The molecular mass of the peptide as assessed by mass spectrometry was 6433 center dot 8 Da. An isoelectric point of 9 center dot 8 was determined by 2D-PAGE. The peptide designated rhamnosin A inhibited Micrococcus lysodeikticus ATCC 4698 but did not inhibit Lactobacillus plantarum 8014 or Lact. plantarum 39268. Inhibitory activity against M. lysodeikticus at concentrations used in this study was shown to be bacteriostatic rather than bacteriolytic or bactericidal. Rhamnosin A retained biological activity after heat treatment (95 degrees C, 30 min) but was sensitive to proteolytic activity of pepsin and trypsin. Conclusions: The N-terminal sequence of rhamnosin A, as determined by Edman degradation and in more detail by blast analysis, did not show identity with any currently available Lact. rhamnosus HN001-translated protein sequences, nor any significant similarity with other sequences in the nonredundant protein sequence database. Being a small, heat-stable, nonlanthionine-containing peptide, rhamnosin A should be categorized as a class II bacteriocin. Significance and Impact of the Study: This study describes a partial bacteriocin sequence isolated from Lact. rhamnosus 68 and broadens our understanding of bacteriocins.en
dc.publisherWiley, Hoboken
dc.relationinfo:eu-repo/grantAgreement/MESTD/MPN2006-2010/142020/RS//
dc.rightsopenAccess
dc.sourceJournal of Applied Microbiology
dc.subjectbacteriocinen
dc.subjectclass IIen
dc.subjectisolationen
dc.subjectLactobacillus rhamnosusen
dc.subjectrhamnosin Aen
dc.titleThe identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68en
dc.typearticle
dc.rights.licenseARR
dc.citation.epage2115
dc.citation.issue6
dc.citation.other107(6): 2108-2115
dc.citation.rankM22
dc.citation.spage2108
dc.citation.volume107
dc.identifier.doi10.1111/j.1365-2672.2009.04539.x
dc.identifier.fulltexthttp://intor.torlakinstitut.com/bitstream/id/133/272.pdf
dc.identifier.pmid19796123
dc.identifier.rcubconv_244
dc.identifier.scopus2-s2.0-72849108588
dc.identifier.wos000271785400037
dc.type.versionpublishedVersion


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