Antibacterial activity and mechanism of phillyrin against selected four foodborne pathogens

Detalhes bibliográficos
Autor(a) principal: ZHANG,Junshun
Data de Publicação: 2022
Outros Autores: GAO,Mingkun, LUO,Jiayuan, GUO,Yang, BAO,Yihong, YANG,Tianzhi
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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spelling 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
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dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000101219
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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
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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)
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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)
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