Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | , , , |
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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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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7160 |
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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 |
repository.mail.fl_str_mv |
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1799135550839455744 |