Inhibitory effects of L-3-phenyllacitc acid on the activity of mushnroom pholyphenol oxidase
Autor(a) principal: | |
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Data de Publicação: | 2021 |
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=S0101-20612021000500343 |
Resumo: | Abstract Polyphenol oxidase is the popular enzyme involved in fruit-vegetable browning and melanin synthesis. In the present paper, L-3-phenyllactic acid, a natural bacteriostatic substance, was investigated as an inhibitor of polyphenol oxidase. The results were demonstrated that the residual enzyme activity of polyphenol oxidase decreased gradually with the increase of the concentration of L-3-phenyllactic acid. The L and ΔE values of the reaction system increased gradually. The reversible mixed-type inhibition mode of L-3-phenyllactic acid was determined by Lineweaver Burk plot. At the same time, the results of fluorescence quenching demonstrated that L-3-phenyllactic acid was a quencher of polyphenol oxidase, and the molecular docking study provided the binding mode of L-3-phenyllactic acid and polyphenol oxidase at the molecular level. L-3-phenyllactic acid decreased the activity of polyphenol oxidase and browning of fresh-cut Agaricus Bosporus. This research first studied the inhibitory effect of L-3-phenyllactic acid on the activity of polyphenol oxidase, and would provide a theoretical foundation for the use of L-3-phenyllactic acid as anti-polyphenol oxidase agents. |
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Inhibitory effects of L-3-phenyllacitc acid on the activity of mushnroom pholyphenol oxidaseL-3-phenyllactic acidmushroom polyphenol oxidaseinhibition kineticsfluorescence quenchingmolecular dockingAbstract Polyphenol oxidase is the popular enzyme involved in fruit-vegetable browning and melanin synthesis. In the present paper, L-3-phenyllactic acid, a natural bacteriostatic substance, was investigated as an inhibitor of polyphenol oxidase. The results were demonstrated that the residual enzyme activity of polyphenol oxidase decreased gradually with the increase of the concentration of L-3-phenyllactic acid. The L and ΔE values of the reaction system increased gradually. The reversible mixed-type inhibition mode of L-3-phenyllactic acid was determined by Lineweaver Burk plot. At the same time, the results of fluorescence quenching demonstrated that L-3-phenyllactic acid was a quencher of polyphenol oxidase, and the molecular docking study provided the binding mode of L-3-phenyllactic acid and polyphenol oxidase at the molecular level. L-3-phenyllactic acid decreased the activity of polyphenol oxidase and browning of fresh-cut Agaricus Bosporus. This research first studied the inhibitory effect of L-3-phenyllactic acid on the activity of polyphenol oxidase, and would provide a theoretical foundation for the use of L-3-phenyllactic acid as anti-polyphenol oxidase agents.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2021-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612021000500343Food Science and Technology v.41 suppl.1 2021reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/fst.08420info:eu-repo/semantics/openAccessREN,HaiweiDU,NanaNIU,XiaoqianWANG,YonggangTIAN,HuiCAO,YingyingZHANG,BinyunFAN,Wenguangeng2021-06-11T00:00:00Zoai:scielo:S0101-20612021000500343Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2021-06-11T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false |
dc.title.none.fl_str_mv |
Inhibitory effects of L-3-phenyllacitc acid on the activity of mushnroom pholyphenol oxidase |
title |
Inhibitory effects of L-3-phenyllacitc acid on the activity of mushnroom pholyphenol oxidase |
spellingShingle |
Inhibitory effects of L-3-phenyllacitc acid on the activity of mushnroom pholyphenol oxidase REN,Haiwei L-3-phenyllactic acid mushroom polyphenol oxidase inhibition kinetics fluorescence quenching molecular docking |
title_short |
Inhibitory effects of L-3-phenyllacitc acid on the activity of mushnroom pholyphenol oxidase |
title_full |
Inhibitory effects of L-3-phenyllacitc acid on the activity of mushnroom pholyphenol oxidase |
title_fullStr |
Inhibitory effects of L-3-phenyllacitc acid on the activity of mushnroom pholyphenol oxidase |
title_full_unstemmed |
Inhibitory effects of L-3-phenyllacitc acid on the activity of mushnroom pholyphenol oxidase |
title_sort |
Inhibitory effects of L-3-phenyllacitc acid on the activity of mushnroom pholyphenol oxidase |
author |
REN,Haiwei |
author_facet |
REN,Haiwei DU,Nana NIU,Xiaoqian WANG,Yonggang TIAN,Hui CAO,Yingying ZHANG,Binyun FAN,Wenguang |
author_role |
author |
author2 |
DU,Nana NIU,Xiaoqian WANG,Yonggang TIAN,Hui CAO,Yingying ZHANG,Binyun FAN,Wenguang |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
REN,Haiwei DU,Nana NIU,Xiaoqian WANG,Yonggang TIAN,Hui CAO,Yingying ZHANG,Binyun FAN,Wenguang |
dc.subject.por.fl_str_mv |
L-3-phenyllactic acid mushroom polyphenol oxidase inhibition kinetics fluorescence quenching molecular docking |
topic |
L-3-phenyllactic acid mushroom polyphenol oxidase inhibition kinetics fluorescence quenching molecular docking |
description |
Abstract Polyphenol oxidase is the popular enzyme involved in fruit-vegetable browning and melanin synthesis. In the present paper, L-3-phenyllactic acid, a natural bacteriostatic substance, was investigated as an inhibitor of polyphenol oxidase. The results were demonstrated that the residual enzyme activity of polyphenol oxidase decreased gradually with the increase of the concentration of L-3-phenyllactic acid. The L and ΔE values of the reaction system increased gradually. The reversible mixed-type inhibition mode of L-3-phenyllactic acid was determined by Lineweaver Burk plot. At the same time, the results of fluorescence quenching demonstrated that L-3-phenyllactic acid was a quencher of polyphenol oxidase, and the molecular docking study provided the binding mode of L-3-phenyllactic acid and polyphenol oxidase at the molecular level. L-3-phenyllactic acid decreased the activity of polyphenol oxidase and browning of fresh-cut Agaricus Bosporus. This research first studied the inhibitory effect of L-3-phenyllactic acid on the activity of polyphenol oxidase, and would provide a theoretical foundation for the use of L-3-phenyllactic acid as anti-polyphenol oxidase agents. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-06-01 |
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=S0101-20612021000500343 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612021000500343 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/fst.08420 |
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.41 suppl.1 2021 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 |
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1752126328630411264 |