Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production
- Autores
- Coscueta, Ezequiel Ricardo; Campos, Débora; Osório, Hugo; Nerli, Bibiana Beatriz; Pintado, Maria Manuela
- Año de publicación
- 2019
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 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.
Fil: Coscueta, Ezequiel Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; Argentina. Universidade Católica Portuguesa; Portugal
Fil: Campos, Débora. Universidade Católica Portuguesa; Portugal
Fil: Osório, Hugo. Universidad de Porto; Portugal
Fil: Nerli, Bibiana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; Argentina
Fil: Pintado, Maria Manuela. Universidade Católica Portuguesa; Portugal - Materia
-
ACE INHIBITOR
ANTIOXIDANT ACTIVITY
BIOACTIVE PEPTIDES
ENZYMATIC HYDROLYSIS
SIMULATED GASTROINTESTINAL DIGESTION
SOY PROTEIN - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/120116
Ver los metadatos del registro completo
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Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient productionCoscueta, Ezequiel RicardoCampos, DéboraOsório, HugoNerli, Bibiana BeatrizPintado, Maria ManuelaACE INHIBITORANTIOXIDANT ACTIVITYBIOACTIVE PEPTIDESENZYMATIC HYDROLYSISSIMULATED GASTROINTESTINAL DIGESTIONSOY PROTEINhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2This 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.Fil: Coscueta, Ezequiel Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; Argentina. Universidade Católica Portuguesa; PortugalFil: Campos, Débora. Universidade Católica Portuguesa; PortugalFil: Osório, Hugo. Universidad de Porto; PortugalFil: Nerli, Bibiana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; ArgentinaFil: Pintado, Maria Manuela. Universidade Católica Portuguesa; PortugalElsevier2019-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/120116Coscueta, Ezequiel Ricardo; Campos, Débora; Osório, Hugo; Nerli, Bibiana Beatriz; Pintado, Maria Manuela; Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production; Elsevier; Food Chemistry: X; 1; 3-2019; 792-804; 100006-1000062590-15750268-005XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S2590157519300082info:eu-repo/semantics/altIdentifier/doi/10.1016/j.fochx.2019.100006info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:32:33Zoai:ri.conicet.gov.ar:11336/120116instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:32:33.346CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
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, Ezequiel Ricardo 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 |
dc.creator.none.fl_str_mv |
Coscueta, Ezequiel Ricardo Campos, Débora Osório, Hugo Nerli, Bibiana Beatriz Pintado, Maria Manuela |
author |
Coscueta, Ezequiel Ricardo |
author_facet |
Coscueta, Ezequiel Ricardo Campos, Débora Osório, Hugo Nerli, Bibiana Beatriz Pintado, Maria Manuela |
author_role |
author |
author2 |
Campos, Débora Osório, Hugo Nerli, Bibiana Beatriz Pintado, Maria Manuela |
author2_role |
author author author author |
dc.subject.none.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 |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
dc.description.none.fl_txt_mv |
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. Fil: Coscueta, Ezequiel Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; Argentina. Universidade Católica Portuguesa; Portugal Fil: Campos, Débora. Universidade Católica Portuguesa; Portugal Fil: Osório, Hugo. Universidad de Porto; Portugal Fil: Nerli, Bibiana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; Argentina Fil: Pintado, Maria Manuela. Universidade Católica Portuguesa; Portugal |
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 |
2019-03 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/120116 Coscueta, Ezequiel Ricardo; Campos, Débora; Osório, Hugo; Nerli, Bibiana Beatriz; Pintado, Maria Manuela; Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production; Elsevier; Food Chemistry: X; 1; 3-2019; 792-804; 100006-100006 2590-1575 0268-005X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/120116 |
identifier_str_mv |
Coscueta, Ezequiel Ricardo; Campos, Débora; Osório, Hugo; Nerli, Bibiana Beatriz; Pintado, Maria Manuela; Enzymatic soy protein hydrolysis: A tool for biofunctional food ingredient production; Elsevier; Food Chemistry: X; 1; 3-2019; 792-804; 100006-100006 2590-1575 0268-005X CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S2590157519300082 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.fochx.2019.100006 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
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:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1844614339091234816 |
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13.070432 |