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

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...

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Institution:Universidad EIA
Main Authors: Pedroza, Carmen Julia, Florez, Alvaro M., Ruiz, Orlando S., Orduz, Sergio
Format: Artículo de revista
Language:English
Published: 2014-01
Subjects:
Quorum sensing
Quorum quenching
AHL-lactonase
N-acyl homoserine lactone
Online Access:https://repositorio.udes.edu.co/handle/001/3566
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id oai:null:001-3566
recordtype dspace
spelling Pedroza, Carmen Julia
Florez, Alvaro M.
Ruiz, Orlando S.
Orduz, Sergio
2019-08-09T18:08:24Z
2019-08-09T18:08:24Z
2014-01
12 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/pdf
10.1007/s10482-013-0072-5
1572-9699
0003-6072
https://repositorio.udes.edu.co/handle/001/3566
eng
Antonie van Leeuwenhoek
Derechos Reservados - Universidad de Santander, 2014
info:eu-repo/semantics/openAccess
Atribución-NoComercial 4.0 Internacional (CC BY-NC 4.0)
https://creativecommons.org/licenses/by-nc/4.0/
https://link.springer.com/article/10.1007%2Fs10482-013-0072-5
Quorum sensing
Quorum quenching
AHL-lactonase
N-acyl homoserine lactone
Enzymatic hydrolysis of molecules associated with bacterial quorum sensing using an acyl homoserine lactonase from a novel Bacillus thuringiensis strain
Artículo de revista
http://purl.org/coar/resource_type/c_6501
Text
info:eu-repo/semantics/article
http://purl.org/redcol/resource_type/ART
info:eu-repo/semantics/publishedVersion
Publication
http://purl.org/coar/access_right/c_abf2
http://purl.org/coar/version/c_970fb48d4fbd8a85
institution Universidad EIA
collection d_repositorio.udes.edu.co-DSPACE
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
Pedroza, Carmen Julia
Florez, Alvaro M.
Ruiz, Orlando S.
Orduz, Sergio
Pedroza, Carmen Julia
Florez, Alvaro M.
Ruiz, Orlando S.
Orduz, Sergio
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
author Pedroza, Carmen Julia
Florez, Alvaro M.
Ruiz, Orlando S.
Orduz, Sergio
Pedroza, Carmen Julia
Florez, Alvaro M.
Ruiz, Orlando S.
Orduz, Sergio
author_facet Pedroza, Carmen Julia
Florez, Alvaro M.
Ruiz, Orlando S.
Orduz, Sergio
Pedroza, Carmen Julia
Florez, Alvaro M.
Ruiz, Orlando S.
Orduz, Sergio
building Repositorio digital
topic Quorum sensing
Quorum quenching
AHL-lactonase
N-acyl homoserine lactone
topic_facet Quorum sensing
Quorum quenching
AHL-lactonase
N-acyl homoserine lactone
publishDate 2014-01
language English
format Artículo de revista
description 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.
issn 1572-9699
url https://repositorio.udes.edu.co/handle/001/3566
url_str_mv https://repositorio.udes.edu.co/handle/001/3566
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score 11.255509