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Enzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain

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dc.contributor.authorPedroza, Carmen Juliaspa
dc.contributor.authorFlorez, Alvaro M.spa
dc.contributor.authorRuiz, Orlando S.spa
dc.contributor.authorOrduz, Sergiospa
dc.date.accessioned2019-08-09T18:08:24Zspa
dc.date.available2019-08-09T18:08:24Zspa
dc.date.issued2014-01spa
dc.description12 p.spa
dc.description.abstractN-acyl homoserine lactones are key components of quorum sensing, the bacterial communication system. This communication mechanism regulates the expression of genes, including those involved in virulence and biofilm formation. This system can be interrupted by the action of enzymes that hydrolyze the signaling molecules. In this work, we studied the enzymatic properties of a recombinant AHL-lactonase from Bacillus thuringiensis strain 147-11516, using substrates with acyl chains of different length (C4-HSL, C6-HSL, C7-HSL, C8-HSL and C10-HSL), we also investigated the effect of pH (5.0–9.0), temperature (20–70 °C), concentration of monovalent, divalent and trivalent metals ions (0.2 and 2.0 mM) and EDTA. The results showed that the recombinant AHL-lactonase had biological activity in alkaline pH conditions (8.0) and high temperature (47 % of hydrolyzed substrate at 60 °C). The recombinant AHL-lactonase has activity on substrates with different acyl chain length. However, the activity of the recombinant enzyme was decreased in the two concentrations of all metal ions evaluated but was not inhibited by EDTA. The affinity of the enzyme for all substrates tested and its performance, in the evaluated conditions, suggest that the AHL-lactonase from B. thuringiensis strain 147-11516 could be used as a strategy for disruption of the Gram-negative bacteria communication system under normal and challenging conditions.eng
dc.format.mimetypeapplication/pdfspa
dc.identifier.doi10.1007/s10482-013-0072-5spa
dc.identifier.issn1572-9699spa
dc.identifier.issn0003-6072spa
dc.identifier.urihttps://repositorio.udes.edu.co/handle/001/3566spa
dc.language.isoengspa
dc.relation.ispartofAntonie van Leeuwenhoekspa
dc.rightsDerechos Reservados - Universidad de Santander, 2014spa
dc.rights.accessrightsinfo:eu-repo/semantics/openAccessspa
dc.rights.creativecommonsAtribución-NoComercial 4.0 Internacional (CC BY-NC 4.0)spa
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0/spa
dc.sourcehttps://link.springer.com/article/10.1007%2Fs10482-013-0072-5spa
dc.subject.proposalQuorum sensingeng
dc.subject.proposalQuorum quenchingeng
dc.subject.proposalAHL-lactonaseeng
dc.subject.proposalN-acyl homoserine lactoneeng
dc.titleEnzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis straineng
dc.typeArtículo de revistaspa
dc.type.coarhttp://purl.org/coar/resource_type/c_6501spa
dc.type.contentTextspa
dc.type.driverinfo:eu-repo/semantics/articlespa
dc.type.redcolhttp://purl.org/redcol/resource_type/ARTspa
dc.type.versioninfo:eu-repo/semantics/publishedVersionspa
dspace.entity.typePublication
oaire.accessrightshttp://purl.org/coar/access_right/c_abf2spa
oaire.versionhttp://purl.org/coar/version/c_970fb48d4fbd8a85spa
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