Antibacterial activity and mechanism of phillyrin against selected four foodborne pathogens
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Food Science and Technology (Campinas) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000101219 |
Resumo: | Abstract The antibacterial activity of phillyrin on Escherichia coli ATCC8739 (E. coli ATCC8739), Bacillus subtilis BS08, Staphylococcus aureus ATCC6538 (S. aureus ATCC6538) and Salmonella ATCC14028 was determined by filter paper method. The minimum inhibitory concentration (MIC) of the four tested bacteria was investigated by plate coating method to evaluate antibacterial ability. The antibacterial mechanism was further investigated by measuring growth curve, electric conductivity, nucleic acid content, Na+/K+-ATPase activity and polyacrylamide gel electrophoresis (SDS-PAGE). The results indicated that phillyrin had antibacterial effects and the MICs against Escherichia coli ATCC8739, Bacillus subtilis BS08, Staphylococcus aureus ATCC6538 and Salmonella ATCC14028 were 2.15, 3.16, 3.02 and 3.40 μg/mL respectively, and the antibacterial effect on Escherichia coli ATCC 8739 was more significant (p< 0.05) than that on other bacteria. Scanning electron microscopy (SEM) indicated that phillyrin destroyed the morphology of the cells and the cells ruptured. The leakage of intracellular substances led to an increase in nucleic acid content and an increase in electric conductivity in the bacterial suspension; SDS-PAGE analysis indicated that phillyrin could inhibit protein synthesis; in addition, phillyrin could reduce Na+/K+-ATPase activity. Therefore, phillyrin had obvious antibacterial ability and inhibited the expression of bacterial proteins by destroying the cell membrane structure, resulting in the death of the cells. |
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Food Science and Technology (Campinas) |
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Antibacterial activity and mechanism of phillyrin against selected four foodborne pathogensphillyrinantibacterial mechanismantibacterial activityAbstract The antibacterial activity of phillyrin on Escherichia coli ATCC8739 (E. coli ATCC8739), Bacillus subtilis BS08, Staphylococcus aureus ATCC6538 (S. aureus ATCC6538) and Salmonella ATCC14028 was determined by filter paper method. The minimum inhibitory concentration (MIC) of the four tested bacteria was investigated by plate coating method to evaluate antibacterial ability. The antibacterial mechanism was further investigated by measuring growth curve, electric conductivity, nucleic acid content, Na+/K+-ATPase activity and polyacrylamide gel electrophoresis (SDS-PAGE). The results indicated that phillyrin had antibacterial effects and the MICs against Escherichia coli ATCC8739, Bacillus subtilis BS08, Staphylococcus aureus ATCC6538 and Salmonella ATCC14028 were 2.15, 3.16, 3.02 and 3.40 μg/mL respectively, and the antibacterial effect on Escherichia coli ATCC 8739 was more significant (p< 0.05) than that on other bacteria. Scanning electron microscopy (SEM) indicated that phillyrin destroyed the morphology of the cells and the cells ruptured. The leakage of intracellular substances led to an increase in nucleic acid content and an increase in electric conductivity in the bacterial suspension; SDS-PAGE analysis indicated that phillyrin could inhibit protein synthesis; in addition, phillyrin could reduce Na+/K+-ATPase activity. Therefore, phillyrin had obvious antibacterial ability and inhibited the expression of bacterial proteins by destroying the cell membrane structure, resulting in the death of the cells.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2022-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000101219Food Science and Technology v.42 2022reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/fst.32922info:eu-repo/semantics/openAccessZHANG,JunshunGAO,MingkunLUO,JiayuanGUO,YangBAO,YihongYANG,Tianzhieng2022-06-30T00:00:00Zoai:scielo:S0101-20612022000101219Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2022-06-30T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false |
dc.title.none.fl_str_mv |
Antibacterial activity and mechanism of phillyrin against selected four foodborne pathogens |
title |
Antibacterial activity and mechanism of phillyrin against selected four foodborne pathogens |
spellingShingle |
Antibacterial activity and mechanism of phillyrin against selected four foodborne pathogens ZHANG,Junshun phillyrin antibacterial mechanism antibacterial activity |
title_short |
Antibacterial activity and mechanism of phillyrin against selected four foodborne pathogens |
title_full |
Antibacterial activity and mechanism of phillyrin against selected four foodborne pathogens |
title_fullStr |
Antibacterial activity and mechanism of phillyrin against selected four foodborne pathogens |
title_full_unstemmed |
Antibacterial activity and mechanism of phillyrin against selected four foodborne pathogens |
title_sort |
Antibacterial activity and mechanism of phillyrin against selected four foodborne pathogens |
author |
ZHANG,Junshun |
author_facet |
ZHANG,Junshun GAO,Mingkun LUO,Jiayuan GUO,Yang BAO,Yihong YANG,Tianzhi |
author_role |
author |
author2 |
GAO,Mingkun LUO,Jiayuan GUO,Yang BAO,Yihong YANG,Tianzhi |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
ZHANG,Junshun GAO,Mingkun LUO,Jiayuan GUO,Yang BAO,Yihong YANG,Tianzhi |
dc.subject.por.fl_str_mv |
phillyrin antibacterial mechanism antibacterial activity |
topic |
phillyrin antibacterial mechanism antibacterial activity |
description |
Abstract The antibacterial activity of phillyrin on Escherichia coli ATCC8739 (E. coli ATCC8739), Bacillus subtilis BS08, Staphylococcus aureus ATCC6538 (S. aureus ATCC6538) and Salmonella ATCC14028 was determined by filter paper method. The minimum inhibitory concentration (MIC) of the four tested bacteria was investigated by plate coating method to evaluate antibacterial ability. The antibacterial mechanism was further investigated by measuring growth curve, electric conductivity, nucleic acid content, Na+/K+-ATPase activity and polyacrylamide gel electrophoresis (SDS-PAGE). The results indicated that phillyrin had antibacterial effects and the MICs against Escherichia coli ATCC8739, Bacillus subtilis BS08, Staphylococcus aureus ATCC6538 and Salmonella ATCC14028 were 2.15, 3.16, 3.02 and 3.40 μg/mL respectively, and the antibacterial effect on Escherichia coli ATCC 8739 was more significant (p< 0.05) than that on other bacteria. Scanning electron microscopy (SEM) indicated that phillyrin destroyed the morphology of the cells and the cells ruptured. The leakage of intracellular substances led to an increase in nucleic acid content and an increase in electric conductivity in the bacterial suspension; SDS-PAGE analysis indicated that phillyrin could inhibit protein synthesis; in addition, phillyrin could reduce Na+/K+-ATPase activity. Therefore, phillyrin had obvious antibacterial ability and inhibited the expression of bacterial proteins by destroying the cell membrane structure, resulting in the death of the cells. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-01-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000101219 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000101219 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/fst.32922 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos |
publisher.none.fl_str_mv |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos |
dc.source.none.fl_str_mv |
Food Science and Technology v.42 2022 reponame:Food Science and Technology (Campinas) instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) instacron:SBCTA |
instname_str |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) |
instacron_str |
SBCTA |
institution |
SBCTA |
reponame_str |
Food Science and Technology (Campinas) |
collection |
Food Science and Technology (Campinas) |
repository.name.fl_str_mv |
Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) |
repository.mail.fl_str_mv |
||revista@sbcta.org.br |
_version_ |
1752126334702714880 |