Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production

Detalhes bibliográficos
Autor(a) principal: Coscueta, ER
Data de Publicação: 2019
Outros Autores: Campos, DA, Osorio, H, Nerli, BB, Pintado, M
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://hdl.handle.net/10216/136319
Resumo: This work aimed to evaluate the digestive stability of the peptides previously identified from a Corolase PP soy protein hydrolysate (SPH) and to respond to the uncertainty about the merit of controlled hydrolysis. For this purpose, we applied an empirical and theoretical analysis, determining peptide sequences, oxygen radical scavenging (ORAC) and ACE inhibitory (iACE) activities, and the effect of hydrolysis on solubility. Results showed that during digestion most of SPH peptides were degraded as smaller ones. However, both SPH bioactivities improved significantly after digestion (3.9 ± 0.1 µmol TE/mg protein for ORAC and IC 50 = 52 ± 4µg protein/mL for iACE) with similar values for soy protein isolate (SPI). With respect to solubility, the controlled hydrolysis considerably increased this functional property. In conclusion, the results indicated that controlled enzymatic hydrolysis of SPI with Corolase PP produced an ingredient more apt to be incorporated in certain nutritional or nutraceutical formulations.
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spelling Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient productionACE inhibitorAntioxidant activityBioactive peptidesEnzymatic hydrolysisSimulated gastrointestinal digestionSoy proteinThis work aimed to evaluate the digestive stability of the peptides previously identified from a Corolase PP soy protein hydrolysate (SPH) and to respond to the uncertainty about the merit of controlled hydrolysis. For this purpose, we applied an empirical and theoretical analysis, determining peptide sequences, oxygen radical scavenging (ORAC) and ACE inhibitory (iACE) activities, and the effect of hydrolysis on solubility. Results showed that during digestion most of SPH peptides were degraded as smaller ones. However, both SPH bioactivities improved significantly after digestion (3.9 ± 0.1 µmol TE/mg protein for ORAC and IC 50 = 52 ± 4µg protein/mL for iACE) with similar values for soy protein isolate (SPI). With respect to solubility, the controlled hydrolysis considerably increased this functional property. In conclusion, the results indicated that controlled enzymatic hydrolysis of SPI with Corolase PP produced an ingredient more apt to be incorporated in certain nutritional or nutraceutical formulations.Elsevier20192019-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/10216/136319eng2590-157510.1016/j.fochx.2019.100006Coscueta, ERCampos, DAOsorio, HNerli, BBPintado, Minfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-29T12:40:53Zoai:repositorio-aberto.up.pt:10216/136319Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T23:24:43.174489Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production
title Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production
spellingShingle Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production
Coscueta, ER
ACE inhibitor
Antioxidant activity
Bioactive peptides
Enzymatic hydrolysis
Simulated gastrointestinal digestion
Soy protein
title_short Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production
title_full Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production
title_fullStr Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production
title_full_unstemmed Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production
title_sort Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production
author Coscueta, ER
author_facet Coscueta, ER
Campos, DA
Osorio, H
Nerli, BB
Pintado, M
author_role author
author2 Campos, DA
Osorio, H
Nerli, BB
Pintado, M
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Coscueta, ER
Campos, DA
Osorio, H
Nerli, BB
Pintado, M
dc.subject.por.fl_str_mv ACE inhibitor
Antioxidant activity
Bioactive peptides
Enzymatic hydrolysis
Simulated gastrointestinal digestion
Soy protein
topic ACE inhibitor
Antioxidant activity
Bioactive peptides
Enzymatic hydrolysis
Simulated gastrointestinal digestion
Soy protein
description This work aimed to evaluate the digestive stability of the peptides previously identified from a Corolase PP soy protein hydrolysate (SPH) and to respond to the uncertainty about the merit of controlled hydrolysis. For this purpose, we applied an empirical and theoretical analysis, determining peptide sequences, oxygen radical scavenging (ORAC) and ACE inhibitory (iACE) activities, and the effect of hydrolysis on solubility. Results showed that during digestion most of SPH peptides were degraded as smaller ones. However, both SPH bioactivities improved significantly after digestion (3.9 ± 0.1 µmol TE/mg protein for ORAC and IC 50 = 52 ± 4µg protein/mL for iACE) with similar values for soy protein isolate (SPI). With respect to solubility, the controlled hydrolysis considerably increased this functional property. In conclusion, the results indicated that controlled enzymatic hydrolysis of SPI with Corolase PP produced an ingredient more apt to be incorporated in certain nutritional or nutraceutical formulations.
publishDate 2019
dc.date.none.fl_str_mv 2019
2019-01-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://hdl.handle.net/10216/136319
url https://hdl.handle.net/10216/136319
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 2590-1575
10.1016/j.fochx.2019.100006
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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