Inhibition of lipid peroxidation of Kiwicha (Amaranthus caudatus) hydrolyzed protein using Zebrafish Larvae and Embryos

Autores
Vilcacundo, Rubén; Barrio, Daniel Alejandro; Piñuel, Maria Lucrecia; Boeri, Patricia; Tombari, Andrea Diana; Pinto, Adelita; Welbaum, James; Hernández Ledesma, Blanca; Carrillo, Wilman
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Amaranth protein concentrate (APC) was hydrolyzed under in vitro gastrointestinal conditions. APC proteins were partially degraded by pepsin at pHs 1.2, 2.0, and 3.2. During the intestinal phase (pepsin/pancreatin enzymes at pH 7.0), no polypeptide bands were observed in the gel, suggesting the susceptibility of amaranth proteins to the action of digestive enzymes. The potent in vitro inhibition of lipid peroxidation, shown by the gastric and intestinal digests, was confirmed in the zebrafish larvae, with a 72.86% reduction in oxidation of lipids in the presence of the gastric hydrolysate at pH 2.0, compared to a 95.72% reduction in the presence of the gastrointestinal digest. APC digests were capable of reducing reactive oxygen species (ROS) production in the zebrafish embryo model with a value of fluorescence of 52.5% for the gastric hydrolysate, and 48.4% for the intestinal hydrolysate.
Fil: Vilcacundo, Rubén. Technical University of Ambato; Ecuador
Fil: Barrio, Daniel Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Negro; Argentina
Fil: Piñuel, Maria Lucrecia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Negro; Argentina
Fil: Boeri, Patricia. Universidad Nacional de Río Negro; Argentina
Fil: Tombari, Andrea Diana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Negro; Argentina
Fil: Pinto, Adelita. Universidad Tecnica de Babahoyo; Ecuador
Fil: Welbaum, James. Texas Tech University; Estados Unidos
Fil: Hernández Ledesma, Blanca. Consejo Superior de Investigaciones Científicas; España
Fil: Carrillo, Wilman. Universidad Tecnica de Babahoyo; Ecuador
Materia
KIWICHA
LIPID PEROXIDATION
PROTEIN CONCENTRATE
SIMULATED GASTROINTESTINAL DIGESTION
ZEBRAFISH EMBRYOS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/177529

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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Inhibition of lipid peroxidation of Kiwicha (Amaranthus caudatus) hydrolyzed protein using Zebrafish Larvae and EmbryosVilcacundo, RubénBarrio, Daniel AlejandroPiñuel, Maria LucreciaBoeri, PatriciaTombari, Andrea DianaPinto, AdelitaWelbaum, JamesHernández Ledesma, BlancaCarrillo, WilmanKIWICHALIPID PEROXIDATIONPROTEIN CONCENTRATESIMULATED GASTROINTESTINAL DIGESTIONZEBRAFISH EMBRYOShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Amaranth protein concentrate (APC) was hydrolyzed under in vitro gastrointestinal conditions. APC proteins were partially degraded by pepsin at pHs 1.2, 2.0, and 3.2. During the intestinal phase (pepsin/pancreatin enzymes at pH 7.0), no polypeptide bands were observed in the gel, suggesting the susceptibility of amaranth proteins to the action of digestive enzymes. The potent in vitro inhibition of lipid peroxidation, shown by the gastric and intestinal digests, was confirmed in the zebrafish larvae, with a 72.86% reduction in oxidation of lipids in the presence of the gastric hydrolysate at pH 2.0, compared to a 95.72% reduction in the presence of the gastrointestinal digest. APC digests were capable of reducing reactive oxygen species (ROS) production in the zebrafish embryo model with a value of fluorescence of 52.5% for the gastric hydrolysate, and 48.4% for the intestinal hydrolysate.Fil: Vilcacundo, Rubén. Technical University of Ambato; EcuadorFil: Barrio, Daniel Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Negro; ArgentinaFil: Piñuel, Maria Lucrecia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Negro; ArgentinaFil: Boeri, Patricia. Universidad Nacional de Río Negro; ArgentinaFil: Tombari, Andrea Diana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Negro; ArgentinaFil: Pinto, Adelita. Universidad Tecnica de Babahoyo; EcuadorFil: Welbaum, James. Texas Tech University; Estados UnidosFil: Hernández Ledesma, Blanca. Consejo Superior de Investigaciones Científicas; EspañaFil: Carrillo, Wilman. Universidad Tecnica de Babahoyo; EcuadorMDPI AG2018-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/177529Vilcacundo, Rubén; Barrio, Daniel Alejandro; Piñuel, Maria Lucrecia; Boeri, Patricia; Tombari, Andrea Diana; et al.; Inhibition of lipid peroxidation of Kiwicha (Amaranthus caudatus) hydrolyzed protein using Zebrafish Larvae and Embryos; MDPI AG; Plants; 7; 3; 9-2018; 1-142223-7747CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/2223-7747/7/3/69info:eu-repo/semantics/altIdentifier/doi/10.3390/plants7030069info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:01:24Zoai:ri.conicet.gov.ar:11336/177529instacron: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 10:01:24.887CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Inhibition of lipid peroxidation of Kiwicha (Amaranthus caudatus) hydrolyzed protein using Zebrafish Larvae and Embryos
title Inhibition of lipid peroxidation of Kiwicha (Amaranthus caudatus) hydrolyzed protein using Zebrafish Larvae and Embryos
spellingShingle Inhibition of lipid peroxidation of Kiwicha (Amaranthus caudatus) hydrolyzed protein using Zebrafish Larvae and Embryos
Vilcacundo, Rubén
KIWICHA
LIPID PEROXIDATION
PROTEIN CONCENTRATE
SIMULATED GASTROINTESTINAL DIGESTION
ZEBRAFISH EMBRYOS
title_short Inhibition of lipid peroxidation of Kiwicha (Amaranthus caudatus) hydrolyzed protein using Zebrafish Larvae and Embryos
title_full Inhibition of lipid peroxidation of Kiwicha (Amaranthus caudatus) hydrolyzed protein using Zebrafish Larvae and Embryos
title_fullStr Inhibition of lipid peroxidation of Kiwicha (Amaranthus caudatus) hydrolyzed protein using Zebrafish Larvae and Embryos
title_full_unstemmed Inhibition of lipid peroxidation of Kiwicha (Amaranthus caudatus) hydrolyzed protein using Zebrafish Larvae and Embryos
title_sort Inhibition of lipid peroxidation of Kiwicha (Amaranthus caudatus) hydrolyzed protein using Zebrafish Larvae and Embryos
dc.creator.none.fl_str_mv Vilcacundo, Rubén
Barrio, Daniel Alejandro
Piñuel, Maria Lucrecia
Boeri, Patricia
Tombari, Andrea Diana
Pinto, Adelita
Welbaum, James
Hernández Ledesma, Blanca
Carrillo, Wilman
author Vilcacundo, Rubén
author_facet Vilcacundo, Rubén
Barrio, Daniel Alejandro
Piñuel, Maria Lucrecia
Boeri, Patricia
Tombari, Andrea Diana
Pinto, Adelita
Welbaum, James
Hernández Ledesma, Blanca
Carrillo, Wilman
author_role author
author2 Barrio, Daniel Alejandro
Piñuel, Maria Lucrecia
Boeri, Patricia
Tombari, Andrea Diana
Pinto, Adelita
Welbaum, James
Hernández Ledesma, Blanca
Carrillo, Wilman
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv KIWICHA
LIPID PEROXIDATION
PROTEIN CONCENTRATE
SIMULATED GASTROINTESTINAL DIGESTION
ZEBRAFISH EMBRYOS
topic KIWICHA
LIPID PEROXIDATION
PROTEIN CONCENTRATE
SIMULATED GASTROINTESTINAL DIGESTION
ZEBRAFISH EMBRYOS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Amaranth protein concentrate (APC) was hydrolyzed under in vitro gastrointestinal conditions. APC proteins were partially degraded by pepsin at pHs 1.2, 2.0, and 3.2. During the intestinal phase (pepsin/pancreatin enzymes at pH 7.0), no polypeptide bands were observed in the gel, suggesting the susceptibility of amaranth proteins to the action of digestive enzymes. The potent in vitro inhibition of lipid peroxidation, shown by the gastric and intestinal digests, was confirmed in the zebrafish larvae, with a 72.86% reduction in oxidation of lipids in the presence of the gastric hydrolysate at pH 2.0, compared to a 95.72% reduction in the presence of the gastrointestinal digest. APC digests were capable of reducing reactive oxygen species (ROS) production in the zebrafish embryo model with a value of fluorescence of 52.5% for the gastric hydrolysate, and 48.4% for the intestinal hydrolysate.
Fil: Vilcacundo, Rubén. Technical University of Ambato; Ecuador
Fil: Barrio, Daniel Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Negro; Argentina
Fil: Piñuel, Maria Lucrecia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Negro; Argentina
Fil: Boeri, Patricia. Universidad Nacional de Río Negro; Argentina
Fil: Tombari, Andrea Diana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Río Negro; Argentina
Fil: Pinto, Adelita. Universidad Tecnica de Babahoyo; Ecuador
Fil: Welbaum, James. Texas Tech University; Estados Unidos
Fil: Hernández Ledesma, Blanca. Consejo Superior de Investigaciones Científicas; España
Fil: Carrillo, Wilman. Universidad Tecnica de Babahoyo; Ecuador
description Amaranth protein concentrate (APC) was hydrolyzed under in vitro gastrointestinal conditions. APC proteins were partially degraded by pepsin at pHs 1.2, 2.0, and 3.2. During the intestinal phase (pepsin/pancreatin enzymes at pH 7.0), no polypeptide bands were observed in the gel, suggesting the susceptibility of amaranth proteins to the action of digestive enzymes. The potent in vitro inhibition of lipid peroxidation, shown by the gastric and intestinal digests, was confirmed in the zebrafish larvae, with a 72.86% reduction in oxidation of lipids in the presence of the gastric hydrolysate at pH 2.0, compared to a 95.72% reduction in the presence of the gastrointestinal digest. APC digests were capable of reducing reactive oxygen species (ROS) production in the zebrafish embryo model with a value of fluorescence of 52.5% for the gastric hydrolysate, and 48.4% for the intestinal hydrolysate.
publishDate 2018
dc.date.none.fl_str_mv 2018-09
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/11336/177529
Vilcacundo, Rubén; Barrio, Daniel Alejandro; Piñuel, Maria Lucrecia; Boeri, Patricia; Tombari, Andrea Diana; et al.; Inhibition of lipid peroxidation of Kiwicha (Amaranthus caudatus) hydrolyzed protein using Zebrafish Larvae and Embryos; MDPI AG; Plants; 7; 3; 9-2018; 1-14
2223-7747
CONICET Digital
CONICET
url http://hdl.handle.net/11336/177529
identifier_str_mv Vilcacundo, Rubén; Barrio, Daniel Alejandro; Piñuel, Maria Lucrecia; Boeri, Patricia; Tombari, Andrea Diana; et al.; Inhibition of lipid peroxidation of Kiwicha (Amaranthus caudatus) hydrolyzed protein using Zebrafish Larvae and Embryos; MDPI AG; Plants; 7; 3; 9-2018; 1-14
2223-7747
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/2223-7747/7/3/69
info:eu-repo/semantics/altIdentifier/doi/10.3390/plants7030069
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv MDPI AG
publisher.none.fl_str_mv MDPI AG
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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score 13.070432