Identification of peptides from edible silkworm pupae (Bombyx mori) protein hydrolysates with antioxidant activity

Silkworm (Bombyx mori) pupae is a by-product from the silk industry which is rich in protein. Hydrolysates from silkworm pupae generated using Alcalase®, Prolyve®, Flavourzyme® and Brewers Clarex® proteolytic prepa- rations were characterised. The antioxidant activity of the hydrolysates was investi...

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Detalhes bibliográficos
Autores: Cermeño, María, Bascón Suárez, María del Carmen, Amigo-Benavent, Miryam, Félix Ángel, Manuel, FitzGerald, Richard J.
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2022
País:España
Recursos:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/140889
Acesso em linha:https://hdl.handle.net/11441/140889
https://doi.org/10.1016/j.jff.2022.105052
Access Level:acceso abierto
Palavra-chave:Antioxidant
Bioactive
Bombyx mori
Peptide
Silkworm
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spelling Identification of peptides from edible silkworm pupae (Bombyx mori) protein hydrolysates with antioxidant activityCermeño, MaríaBascón Suárez, María del CarmenAmigo-Benavent, MiryamFélix Ángel, ManuelFitzGerald, Richard J.AntioxidantBioactiveBombyx moriPeptideSilkwormSilkworm (Bombyx mori) pupae is a by-product from the silk industry which is rich in protein. Hydrolysates from silkworm pupae generated using Alcalase®, Prolyve®, Flavourzyme® and Brewers Clarex® proteolytic prepa- rations were characterised. The antioxidant activity of the hydrolysates was investigated using in vitro antioxi- dant assays and an in situ assay for reactive oxygen species (ROS) reduction using hepatic HepG2. Overall, Alcalase and Prolyve hydrolysates had highest scavenging activities, however, Flavourzyme and Brewers Clarex hydrolysates had enhanced ferric reducing antioxidant power (FRAP) activity compared to the other samples. Furthermore, the Flavourzyme hydrolysate significantly reduced ROS by 40% compared to untreated control HepG2 cells. Peptides identified by LC-MS/MS were synthetised and then tested for their in vitro and in situ antioxidant activity. Peptides SWFVTPF and NDVLFF showed highest antioxidant activity (ROS reduction, su- peroxide dismutase (SOD) expression and glutathione (GSH) production activity) in HepG2 cells, and therefore may have potential as natural antioxidants.ElsevierIngeniería QuímicaTEP229: Tecnología y Diseño de Productos MulticomponentesThe Disruptive Technologies Innovation Fund by Enterprise Ireland (DTIF) grant no. DT20180088University of Seville for the VPPI-US grant Ref.-II.5Consejería de Transformación económica, Industria, Conocimiento y Universidades de la Junta de Andalucía-Agencia Andaluza del Conocimiento and FEDER, UE by the grant Ref. PY20_010462022info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/140889https://doi.org/10.1016/j.jff.2022.105052reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésJournal of Functional Foods, 92 (105052).DT20180088VPPI-US Ref.-II.5PY20_01046https://www.sciencedirect.com/science/article/pii/S1756464622001220info:eu-repo/semantics/openAccessoai:idus.us.es:11441/1408892026-06-17T12:51:07Z
dc.title.none.fl_str_mv Identification of peptides from edible silkworm pupae (Bombyx mori) protein hydrolysates with antioxidant activity
title Identification of peptides from edible silkworm pupae (Bombyx mori) protein hydrolysates with antioxidant activity
spellingShingle Identification of peptides from edible silkworm pupae (Bombyx mori) protein hydrolysates with antioxidant activity
Cermeño, María
Antioxidant
Bioactive
Bombyx mori
Peptide
Silkworm
title_short Identification of peptides from edible silkworm pupae (Bombyx mori) protein hydrolysates with antioxidant activity
title_full Identification of peptides from edible silkworm pupae (Bombyx mori) protein hydrolysates with antioxidant activity
title_fullStr Identification of peptides from edible silkworm pupae (Bombyx mori) protein hydrolysates with antioxidant activity
title_full_unstemmed Identification of peptides from edible silkworm pupae (Bombyx mori) protein hydrolysates with antioxidant activity
title_sort Identification of peptides from edible silkworm pupae (Bombyx mori) protein hydrolysates with antioxidant activity
dc.creator.none.fl_str_mv Cermeño, María
Bascón Suárez, María del Carmen
Amigo-Benavent, Miryam
Félix Ángel, Manuel
FitzGerald, Richard J.
author Cermeño, María
author_facet Cermeño, María
Bascón Suárez, María del Carmen
Amigo-Benavent, Miryam
Félix Ángel, Manuel
FitzGerald, Richard J.
author_role author
author2 Bascón Suárez, María del Carmen
Amigo-Benavent, Miryam
Félix Ángel, Manuel
FitzGerald, Richard J.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Ingeniería Química
TEP229: Tecnología y Diseño de Productos Multicomponentes
The Disruptive Technologies Innovation Fund by Enterprise Ireland (DTIF) grant no. DT20180088
University of Seville for the VPPI-US grant Ref.-II.5
Consejería de Transformación económica, Industria, Conocimiento y Universidades de la Junta de Andalucía-Agencia Andaluza del Conocimiento and FEDER, UE by the grant Ref. PY20_01046
dc.subject.none.fl_str_mv Antioxidant
Bioactive
Bombyx mori
Peptide
Silkworm
topic Antioxidant
Bioactive
Bombyx mori
Peptide
Silkworm
description Silkworm (Bombyx mori) pupae is a by-product from the silk industry which is rich in protein. Hydrolysates from silkworm pupae generated using Alcalase®, Prolyve®, Flavourzyme® and Brewers Clarex® proteolytic prepa- rations were characterised. The antioxidant activity of the hydrolysates was investigated using in vitro antioxi- dant assays and an in situ assay for reactive oxygen species (ROS) reduction using hepatic HepG2. Overall, Alcalase and Prolyve hydrolysates had highest scavenging activities, however, Flavourzyme and Brewers Clarex hydrolysates had enhanced ferric reducing antioxidant power (FRAP) activity compared to the other samples. Furthermore, the Flavourzyme hydrolysate significantly reduced ROS by 40% compared to untreated control HepG2 cells. Peptides identified by LC-MS/MS were synthetised and then tested for their in vitro and in situ antioxidant activity. Peptides SWFVTPF and NDVLFF showed highest antioxidant activity (ROS reduction, su- peroxide dismutase (SOD) expression and glutathione (GSH) production activity) in HepG2 cells, and therefore may have potential as natural antioxidants.
publishDate 2022
dc.date.none.fl_str_mv 2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/140889
https://doi.org/10.1016/j.jff.2022.105052
url https://hdl.handle.net/11441/140889
https://doi.org/10.1016/j.jff.2022.105052
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Journal of Functional Foods, 92 (105052).
DT20180088
VPPI-US Ref.-II.5
PY20_01046
https://www.sciencedirect.com/science/article/pii/S1756464622001220
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.301629

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