Enzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain
12 p.
- Autores:
-
Pedroza, Carmen Julia
Florez, Alvaro M.
Ruiz, Orlando S.
Orduz, Sergio
- Tipo de recurso:
- Article of journal
- Fecha de publicación:
- 2014
- Institución:
- Universidad de Santander
- Repositorio:
- Repositorio Universidad de Santander
- Idioma:
- eng
- OAI Identifier:
- oai:repositorio.udes.edu.co:001/3566
- Acceso en línea:
- https://repositorio.udes.edu.co/handle/001/3566
- Palabra clave:
- Quorum sensing
Quorum quenching
AHL-lactonase
N-acyl homoserine lactone
- Rights
- openAccess
- License
- Derechos Reservados - Universidad de Santander, 2014
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Enzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain |
| title |
Enzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain |
| spellingShingle |
Enzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain Quorum sensing Quorum quenching AHL-lactonase N-acyl homoserine lactone |
| title_short |
Enzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain |
| title_full |
Enzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain |
| title_fullStr |
Enzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain |
| title_full_unstemmed |
Enzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain |
| title_sort |
Enzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain |
| dc.creator.fl_str_mv |
Pedroza, Carmen Julia Florez, Alvaro M. Ruiz, Orlando S. Orduz, Sergio |
| dc.contributor.author.spa.fl_str_mv |
Pedroza, Carmen Julia Florez, Alvaro M. Ruiz, Orlando S. Orduz, Sergio |
| dc.subject.proposal.eng.fl_str_mv |
Quorum sensing Quorum quenching AHL-lactonase N-acyl homoserine lactone |
| topic |
Quorum sensing Quorum quenching AHL-lactonase N-acyl homoserine lactone |
| description |
12 p. |
| publishDate |
2014 |
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2014-01 |
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2019-08-09T18:08:24Z |
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2019-08-09T18:08:24Z |
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10.1007/s10482-013-0072-5 |
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1572-9699 0003-6072 |
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https://repositorio.udes.edu.co/handle/001/3566 |
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10.1007/s10482-013-0072-5 1572-9699 0003-6072 |
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| dc.language.iso.spa.fl_str_mv |
eng |
| language |
eng |
| dc.relation.ispartof.spa.fl_str_mv |
Antonie van Leeuwenhoek |
| dc.rights.spa.fl_str_mv |
Derechos Reservados - Universidad de Santander, 2014 |
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Atribución-NoComercial 4.0 Internacional (CC BY-NC 4.0) |
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https://creativecommons.org/licenses/by-nc/4.0/ |
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openAccess |
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application/pdf |
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Pedroza, Carmen Julia923a2f11-d40b-4129-92f7-9f8d53af6feb-1Florez, Alvaro M.03b37924-311e-4ca6-bae7-fb60528ecb1c-1Ruiz, Orlando S.4935a6c8-72b5-4e4d-8963-3a55d7947b9a-1Orduz, Sergiod94079f7-48c0-4449-85b1-539f320c34c9-12019-08-09T18:08:24Z2019-08-09T18:08:24Z2014-0112 p.N-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.application/pdf10.1007/s10482-013-0072-51572-96990003-6072https://repositorio.udes.edu.co/handle/001/3566engAntonie van LeeuwenhoekDerechos Reservados - Universidad de Santander, 2014info:eu-repo/semantics/openAccessAtribución-NoComercial 4.0 Internacional (CC BY-NC 4.0)https://creativecommons.org/licenses/by-nc/4.0/http://purl.org/coar/access_right/c_abf2https://link.springer.com/article/10.1007%2Fs10482-013-0072-5Quorum sensingQuorum quenchingAHL-lactonaseN-acyl homoserine lactoneEnzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strainArtículo de revistahttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1Textinfo:eu-repo/semantics/articlehttp://purl.org/redcol/resource_type/ARTinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/version/c_970fb48d4fbd8a85PublicationBRANDED_PREVIEWEnzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain.PNG.preview.jpgEnzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain.PNG.preview.jpgGenerated Branded Previewimage/jpeg6189https://repositorio.udes.edu.co/bitstreams/b7a2fbe7-b9eb-46e4-b446-7057798b4ed3/download408989ffbc1bb887f63c90497b3bccbdMD54THUMBNAILEnzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain.PNG.jpgEnzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain.PNG.jpgUDESimage/jpeg1518https://repositorio.udes.edu.co/bitstreams/3e47a842-0906-4bb8-b270-f830e8f580dc/downloadd3c1769396ec91d58fd2ba81db9f3246MD53Enzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain.pdf.jpgEnzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain.pdf.jpgGenerated Thumbnailimage/jpeg6239https://repositorio.udes.edu.co/bitstreams/b3fee560-acb2-4aed-9f87-9893debe322f/download42b0136e4368b94a6bcc4229fd8a160bMD57LICENSElicense.txtlicense.txttext/plain; charset=utf-859https://repositorio.udes.edu.co/bitstreams/0dcf394f-33d9-4365-9535-a08d68515573/download38d94cf55aa1bf2dac1a736ac45c881cMD52ORIGINALEnzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain.pdfEnzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain.pdfapplication/pdf238470https://repositorio.udes.edu.co/bitstreams/9c1a46d3-d007-4fbc-824f-defcc8026547/download487ecf48f853ce121289b6fe8bcd423fMD55TEXTEnzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain.pdf.txtEnzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain.pdf.txtExtracted texttext/plain5https://repositorio.udes.edu.co/bitstreams/2a397937-1696-436d-88c2-36749840b6de/download5dbe86c1111d64f45ba435df98fdc825MD56001/3566oai:repositorio.udes.edu.co:001/35662023-10-11 11:08:59.526https://creativecommons.org/licenses/by-nc/4.0/Derechos Reservados - Universidad de Santander, 2014https://repositorio.udes.edu.coRepositorio Universidad de Santandersoporte@metabiblioteca.comTGljZW5jaWEgZGUgUHVibGljYWNpw7NuIFVERVMKRGlyZWN0cmljZXMgZGUgVVNPIHkgQUNDRVNPCgo= |