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Magnetic immobilization of a quorum sensing signal hydrolase, AiiA

Magnetic immobilization of quorum sensing (QS) signal hydrolases provides a convenient solution for quenching QS process that is essential for bacterial biofilm formation and antimicrobial resistance. In the present study, a QS signal hydrolase, AiiA, was fused with a magnetic protein, MagR, and exp...

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Detalles Bibliográficos
Autores principales: Wang, Lin, Xu, Haixing, Liu, Zewen, Sun, Taolei, Yuan, Chengqing, Yang, Ying, Guo, Junhui, Xie, Hao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6692522/
https://www.ncbi.nlm.nih.gov/pubmed/30767416
http://dx.doi.org/10.1002/mbo3.797
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author Wang, Lin
Xu, Haixing
Liu, Zewen
Sun, Taolei
Yuan, Chengqing
Yang, Ying
Guo, Junhui
Xie, Hao
author_facet Wang, Lin
Xu, Haixing
Liu, Zewen
Sun, Taolei
Yuan, Chengqing
Yang, Ying
Guo, Junhui
Xie, Hao
author_sort Wang, Lin
collection PubMed
description Magnetic immobilization of quorum sensing (QS) signal hydrolases provides a convenient solution for quenching QS process that is essential for bacterial biofilm formation and antimicrobial resistance. In the present study, a QS signal hydrolase, AiiA, was fused with a magnetic protein, MagR, and expressed in Escherichia coli. Magnetic immobilization of AiiA was achieved on Fe(3)O(4)‐SiO(2) iron beads and was confirmed via SDS‐PAGE, zeta potential measurement, FTIR spectrometry, and SEM analysis. The magnetic immobilized AiiA exhibited activity in degrading the quorum sensing signal, C6‐HSL. This study opens a new avenue to actively immobilize enzymes via magnetic interaction and quench quorum sensing.
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spelling pubmed-66925222019-08-16 Magnetic immobilization of a quorum sensing signal hydrolase, AiiA Wang, Lin Xu, Haixing Liu, Zewen Sun, Taolei Yuan, Chengqing Yang, Ying Guo, Junhui Xie, Hao Microbiologyopen Original Articles Magnetic immobilization of quorum sensing (QS) signal hydrolases provides a convenient solution for quenching QS process that is essential for bacterial biofilm formation and antimicrobial resistance. In the present study, a QS signal hydrolase, AiiA, was fused with a magnetic protein, MagR, and expressed in Escherichia coli. Magnetic immobilization of AiiA was achieved on Fe(3)O(4)‐SiO(2) iron beads and was confirmed via SDS‐PAGE, zeta potential measurement, FTIR spectrometry, and SEM analysis. The magnetic immobilized AiiA exhibited activity in degrading the quorum sensing signal, C6‐HSL. This study opens a new avenue to actively immobilize enzymes via magnetic interaction and quench quorum sensing. John Wiley and Sons Inc. 2019-02-14 /pmc/articles/PMC6692522/ /pubmed/30767416 http://dx.doi.org/10.1002/mbo3.797 Text en © 2019 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Articles
Wang, Lin
Xu, Haixing
Liu, Zewen
Sun, Taolei
Yuan, Chengqing
Yang, Ying
Guo, Junhui
Xie, Hao
Magnetic immobilization of a quorum sensing signal hydrolase, AiiA
title Magnetic immobilization of a quorum sensing signal hydrolase, AiiA
title_full Magnetic immobilization of a quorum sensing signal hydrolase, AiiA
title_fullStr Magnetic immobilization of a quorum sensing signal hydrolase, AiiA
title_full_unstemmed Magnetic immobilization of a quorum sensing signal hydrolase, AiiA
title_short Magnetic immobilization of a quorum sensing signal hydrolase, AiiA
title_sort magnetic immobilization of a quorum sensing signal hydrolase, aiia
topic Original Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6692522/
https://www.ncbi.nlm.nih.gov/pubmed/30767416
http://dx.doi.org/10.1002/mbo3.797
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