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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/177529
Ver los metadatos del registro completo
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oai:ri.conicet.gov.ar:11336/177529 |
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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 |
_version_ |
1844613807368830976 |
score |
13.070432 |