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dc.contributor.authorVaičikauskaitė, Manta
dc.contributor.authorGer, Marija
dc.contributor.authorValius, Mindaugas
dc.contributor.authorManeikis, Andrius
dc.contributor.authorLastauskienė, Eglė
dc.contributor.authorKalėdienė, Lilija
dc.contributor.authorKaunietis, Arnoldas
dc.date.accessioned2023-09-18T20:13:42Z
dc.date.available2023-09-18T20:13:42Z
dc.date.issued2019
dc.identifier.issn0141-8130
dc.identifier.urihttps://etalpykla.vilniustech.lt/handle/123456789/147745
dc.description.abstractBacteriocins are ribosomally synthesized peptides/proteins produced by bacteria. These compounds have antibacterial activity against other bacteria that are usually closely related to the producer strain. Here we describe bacteriocin geobacillin 26 from a thermophilic Gram-positive bacterium Geobacillus stearothermophilus 15. We have purified native bacteriocin, determined its amino acid sequence and heterologously expressed in Gram-negative Escherichia coli. Geobacillin 26 is a heat-labile, high molecular weight antibacterial protein belonging to class III bacteriocins. It has a narrow antibacterial spectrum against other thermophilic bacteria. Our study suggests that this bacteriocin is not a cell wall hydrolyzing enzyme as most of high molecular weight bacteriocins. In addition, geobacillin 26 has no amino acid sequence similarities to other known function proteins. No other class III bacteriocin from a thermophilic bacterium has been reported and well characterized before. Geobacillin 26 as a natural antibacterial agent has a great potential in industry where contamination with other thermophilic bacteria is unwanted. Moreover, this study may prompt to disclose more novel geobacillin 26-like antibacterial proteins, which could find their applications in food industry or medicine.eng
dc.formatPDF
dc.format.extentp. 333-344
dc.format.mediumtekstas / txt
dc.language.isoeng
dc.relation.isreferencedbyEmbase
dc.relation.isreferencedbyPubMed
dc.relation.isreferencedbyScopus
dc.relation.isreferencedbyScience Citation Index Expanded (Web of Science)
dc.source.urihttps://www.sciencedirect.com/science/article/pii/S0141813019352092?via%3Dihub
dc.source.urihttps://doi.org/10.1016/j.ijbiomac.2019.09.047
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID...
dc.titleGeobacillin 26 - high molecular weight bacteriocin from a thermophilic bacterium
dc.typeStraipsnis Web of Science DB / Article in Web of Science DB
dcterms.references51
dc.type.pubtypeS1 - Straipsnis Web of Science DB / Web of Science DB article
dc.contributor.institutionVilniaus universitetas
dc.contributor.institutionVilniaus Gedimino technikos universitetas
dc.contributor.facultyElektronikos fakultetas / Faculty of Electronics
dc.subject.researchfieldN 010 - Biologija / Biology
dc.subject.researchfieldT 008 - Medžiagų inžinerija / Material engineering
dc.subject.vgtuprioritizedfieldsFM0202 - Ląstelių ir jų biologiškai aktyvių komponentų tyrimai / Investigations on cells and their biologically active components
dc.subject.ltspecializationsL105 - Sveikatos technologijos ir biotechnologijos / Health technologies and biotechnologies
dc.subject.enantibacterial protein
dc.subject.enbacteriocin
dc.subject.engeobacillus
dc.subject.enthermophilic bacteria
dcterms.sourcetitleInternational journal of biological macromolecules
dc.description.volumevol. 141
dc.publisher.nameElsevier
dc.publisher.cityAmsterdam
dc.identifier.doi2-s2.0-85071859285
dc.identifier.doiS0141813019352092
dc.identifier.doi85071859285
dc.identifier.doi0
dc.identifier.doi000506713000035
dc.identifier.doi10.1016/j.ijbiomac.2019.09.047
dc.identifier.elaba41248719


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