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Inhibitory mechanism of quercetin on Alicyclobacillus acidoterrestris
In this the antibacterial of quercetin against Alicyclobacillus acidoterrestris was evaluated by measuring the minimal inhibitory concentration (MIC) and minimal bactericidal concentration (MBC). Subsequently, the effect of quercetin on A. acidoterrestris cell membrane was evaluated through scanning...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10684910/ https://www.ncbi.nlm.nih.gov/pubmed/38033555 http://dx.doi.org/10.3389/fmicb.2023.1286187 |
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author | Liang, Xinhong Tu, Cunjian Li, Yongchao Sun, Junliang Zhao, Ruixiang Ran, Junjian Jiao, Lingxia Huang, Junchao Li, Junrui |
author_facet | Liang, Xinhong Tu, Cunjian Li, Yongchao Sun, Junliang Zhao, Ruixiang Ran, Junjian Jiao, Lingxia Huang, Junchao Li, Junrui |
author_sort | Liang, Xinhong |
collection | PubMed |
description | In this the antibacterial of quercetin against Alicyclobacillus acidoterrestris was evaluated by measuring the minimal inhibitory concentration (MIC) and minimal bactericidal concentration (MBC). Subsequently, the effect of quercetin on A. acidoterrestris cell membrane was evaluated through scanning electron microscopy (SEM), surface hydrophobicity determination, diacetate fluorescein staining and propidium iodide (PI) staining. Additionally, the effects of quercetin on intracellular macromolecules and cell metabolism were explored by measuring the culture medium protein, bacterial protein and intracellular sodium and potassium adenosine triphosphate (ATP) enzyme activity. The results revealed that quercetin exhibited the MIC and MBC values of 100 ug/mL and 400 ug/mL, respectively, against A. acidoterrestris. The SEM results revealed that quercetin could induce irreversible damage to the cell membrane effectively. Moreover, quercetin could enhance the surface hydrophobicity of A. acidoterrestris. The results of flow cytometry and fluorescence microscopy analyses revealed that quercetin could promote cell damage by altering the cell membrane permeability of A. acidoterrestris, inducing the release of nucleic acid substances from the cells. Furthermore, the determination of protein content in the culture medium, bacterial protein content, and the Na(+)/K(+)-ATPase activity demonstrated that quercetin could reduce the intracellular protein content and impedes protein expression and ATPase synthesis effectively, leading to apoptosis. |
format | Online Article Text |
id | pubmed-10684910 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-106849102023-11-30 Inhibitory mechanism of quercetin on Alicyclobacillus acidoterrestris Liang, Xinhong Tu, Cunjian Li, Yongchao Sun, Junliang Zhao, Ruixiang Ran, Junjian Jiao, Lingxia Huang, Junchao Li, Junrui Front Microbiol Microbiology In this the antibacterial of quercetin against Alicyclobacillus acidoterrestris was evaluated by measuring the minimal inhibitory concentration (MIC) and minimal bactericidal concentration (MBC). Subsequently, the effect of quercetin on A. acidoterrestris cell membrane was evaluated through scanning electron microscopy (SEM), surface hydrophobicity determination, diacetate fluorescein staining and propidium iodide (PI) staining. Additionally, the effects of quercetin on intracellular macromolecules and cell metabolism were explored by measuring the culture medium protein, bacterial protein and intracellular sodium and potassium adenosine triphosphate (ATP) enzyme activity. The results revealed that quercetin exhibited the MIC and MBC values of 100 ug/mL and 400 ug/mL, respectively, against A. acidoterrestris. The SEM results revealed that quercetin could induce irreversible damage to the cell membrane effectively. Moreover, quercetin could enhance the surface hydrophobicity of A. acidoterrestris. The results of flow cytometry and fluorescence microscopy analyses revealed that quercetin could promote cell damage by altering the cell membrane permeability of A. acidoterrestris, inducing the release of nucleic acid substances from the cells. Furthermore, the determination of protein content in the culture medium, bacterial protein content, and the Na(+)/K(+)-ATPase activity demonstrated that quercetin could reduce the intracellular protein content and impedes protein expression and ATPase synthesis effectively, leading to apoptosis. Frontiers Media S.A. 2023-11-15 /pmc/articles/PMC10684910/ /pubmed/38033555 http://dx.doi.org/10.3389/fmicb.2023.1286187 Text en Copyright © 2023 Liang, Tu, Li, Sun, Zhao, Ran, Jiao, Huang and Li. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Liang, Xinhong Tu, Cunjian Li, Yongchao Sun, Junliang Zhao, Ruixiang Ran, Junjian Jiao, Lingxia Huang, Junchao Li, Junrui Inhibitory mechanism of quercetin on Alicyclobacillus acidoterrestris |
title | Inhibitory mechanism of quercetin on Alicyclobacillus acidoterrestris |
title_full | Inhibitory mechanism of quercetin on Alicyclobacillus acidoterrestris |
title_fullStr | Inhibitory mechanism of quercetin on Alicyclobacillus acidoterrestris |
title_full_unstemmed | Inhibitory mechanism of quercetin on Alicyclobacillus acidoterrestris |
title_short | Inhibitory mechanism of quercetin on Alicyclobacillus acidoterrestris |
title_sort | inhibitory mechanism of quercetin on alicyclobacillus acidoterrestris |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10684910/ https://www.ncbi.nlm.nih.gov/pubmed/38033555 http://dx.doi.org/10.3389/fmicb.2023.1286187 |
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