Extraction of protein concentrate from red bean (Phaseolus vulgaris L.): antioxidant activity and inhibition of lipid peroxidation
- Autores
- Piñuel, María Lucrecia; Vilcacundo, Edgar; Boeri, Patricia Alejandra; Barrio, Daniel Alejandro; Morales, Dayana; Pinto, Adelita; Moran, Roberto; Samaniego, Ivan; Carrillo, Wilman
- Año de publicación
- 2019
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Fil: Piñuel, María L. Universidad Nacional de Río Negro; Argentina
Fil: Vilcacundo, Edgar. Bolivar State University. Department of Research; Ecuador.
Fil: Boeri, Patricia A. Universidad Nacional de Río Negro; Argentina
Fil: Barrio, Daniel A. Universidad Nacional de Río Negro; Argentina
Fil: Morales, Dayana. Technical University of Ambato. Faculty of Science and Engineering in Food and Biotechnology; Ecuador.
Fil: Pinto, Adelita. Technical University of Babahoyo. Department of Research; Ecuador.
Fil: Moran, Roberto. National Institute of Agricultural Research (INIAP). Department of Nutrition and Quality; Ecuador.
Fil: Samaniego, Ivan. National Institute of Agricultural Research (INIAP). Department of Nutrition and Quality; Ecuador.
Fil: Carrillo, Wilman. Technical University of Babahoyo. Department of Research; Ecuador.
Fil: Barrio, Daniel A. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.
Fil: Piñuel, María L. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.
Fil: Boeri, Patricia A. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.
Red Bean Protein Concentrate (RBPC) and their hydrolysates were used to evaluate the antioxidant capacity. The RBPC protein content was in the range of 57.38%–72.68% of the total sample content. RBPC protein profile showed a range of 15–100 kDa. Phaseolin protein was identified with bands of 45 and 50 kDa. Phaseolin protein was found in all the RBPC samples at the different pHs assayed. In the gastric digestion phase, bands from 60 to 100 kDa were totally hydrolyzed with pepsin. Phaseolin protein (45 and 50 kDa) presented resistance to gastric hydrolysis. All the RBPCs and gastrointestinal digest presented antioxidant activity using ferric-reducing antioxidant power (FRAP), 2,2-azinobis (3-ethyl-benzothiazoline-6-sulfonic acid) (ABTS), oxygen radical absorbance capacity (ORAC), and thiobarbituric acid reactive substances using the in vitro and in vivo methods. RBPC at pH 7.0 presented a value of 95.80 μmoL TE/g of RBPC (FRAP); 257.12 μmoL TE/g of RBPC (ABTS), and 1960 μmoL TE/g of RBPC (ORAC). Duodenal digest of RBPC presented high antioxidant activity with 225.77 μmoL TE/g of digest (FRAP); 345.21 μmoL TE/g of digest (ABTS); and 3256 μmoL TE/g of digest (ORAC). Gastric and duodenal digest of RBPC were used to inhibit lipid peroxidation using the in vitro method presenting a value of 87.95% and 93.0%, respectively. When the in vivo method in zebrafish larvae was used, values were 79.03% and 86.76%, respectively. RBPCs showed no reactive oxygen species (ROS) inhibition. However, RBPCs with gastric and gastrointestinal digests, presented ROS inhibition, 75.30% for gastric digests and 66.40% for gastrointestinal digests.
El concentrado de proteína de frijol rojo (RBPC) y sus hidrolizados se usaron para evaluar la capacidad antioxidante. El contenido de proteína RBPC estaba en el rango de 57.38% –72.68% del contenido total de la muestra. El perfil de proteína RBPC mostró un rango de 15 a 100 kDa. La proteína de faseolina se identificó con bandas de 45 y 50 kDa. Se encontró proteína de faseolina en todas las muestras de RBPC a los diferentes pH analizados. En la fase de digestión gástrica, las bandas de 60 a 100 kDa se hidrolizaron totalmente con pepsina. La proteína Phaseolin (45 y 50 kDa) presentó resistencia a la hidrólisis gástrica. Todos los RBPC y el digestivo gastrointestinal presentaron actividad antioxidante utilizando poder antioxidante reductor férrico (FRAP), 2,2-azinobis (ácido 3-etil-benzotiazolina-6-sulfónico) (ABTS), capacidad de absorbancia de radicales de oxígeno (ORAC) y tiobarbitúrico sustancias reactivas al ácido utilizando los métodos in vitro e in vivo. RBPC a pH 7.0 presentó un valor de 95.80 μmoL TE / g de RBPC (FRAP); 257.12 μmoL TE / g de RBPC (ABTS), y 1960 μmoL TE / g de RBPC (ORAC). La digestión duodenal de RBPC presentó una alta actividad antioxidante con 225.77 μmoL TE / g de digestión (FRAP); 345,21 μmoL TE / g de digestión (ABTS); y 3256 μmoL TE / g de digestión (ORAC). La digestión gástrica y duodenal de RBPC se utilizó para inhibir la peroxidación lipídica utilizando el método in vitro que presenta un valor de 87.95% y 93.0%, respectivamente. Cuando se usó el método in vivo en larvas de pez cebra, los valores fueron 79.03% y 86.76%, respectivamente. Las RBPC no mostraron inhibición de especies reactivas de oxígeno (ROS). Sin embargo, las RBPC con digestiones gástricas y gastrointestinales presentaron inhibición de ROS, 75.30% para las digeridas gástricas y 66.40% para las digeridas gastrointestinales. - Materia
-
Common Bean
Phaseolus Vulgaris
Protein Concentrate
Antioxidant Activity
Zebrafish Larvae - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
- Institución
- Universidad Nacional de Río Negro
- OAI Identificador
- oai:rid.unrn.edu.ar:20.500.12049/4480
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Extraction of protein concentrate from red bean (Phaseolus vulgaris L.): antioxidant activity and inhibition of lipid peroxidationPiñuel, María LucreciaVilcacundo, EdgarBoeri, Patricia AlejandraBarrio, Daniel AlejandroMorales, DayanaPinto, AdelitaMoran, RobertoSamaniego, IvanCarrillo, WilmanCommon BeanPhaseolus VulgarisProtein ConcentrateAntioxidant ActivityZebrafish LarvaeFil: Piñuel, María L. Universidad Nacional de Río Negro; ArgentinaFil: Vilcacundo, Edgar. Bolivar State University. Department of Research; Ecuador.Fil: Boeri, Patricia A. Universidad Nacional de Río Negro; ArgentinaFil: Barrio, Daniel A. Universidad Nacional de Río Negro; ArgentinaFil: Morales, Dayana. Technical University of Ambato. Faculty of Science and Engineering in Food and Biotechnology; Ecuador.Fil: Pinto, Adelita. Technical University of Babahoyo. Department of Research; Ecuador.Fil: Moran, Roberto. National Institute of Agricultural Research (INIAP). Department of Nutrition and Quality; Ecuador.Fil: Samaniego, Ivan. National Institute of Agricultural Research (INIAP). Department of Nutrition and Quality; Ecuador.Fil: Carrillo, Wilman. Technical University of Babahoyo. Department of Research; Ecuador.Fil: Barrio, Daniel A. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.Fil: Piñuel, María L. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.Fil: Boeri, Patricia A. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.Red Bean Protein Concentrate (RBPC) and their hydrolysates were used to evaluate the antioxidant capacity. The RBPC protein content was in the range of 57.38%–72.68% of the total sample content. RBPC protein profile showed a range of 15–100 kDa. Phaseolin protein was identified with bands of 45 and 50 kDa. Phaseolin protein was found in all the RBPC samples at the different pHs assayed. In the gastric digestion phase, bands from 60 to 100 kDa were totally hydrolyzed with pepsin. Phaseolin protein (45 and 50 kDa) presented resistance to gastric hydrolysis. All the RBPCs and gastrointestinal digest presented antioxidant activity using ferric-reducing antioxidant power (FRAP), 2,2-azinobis (3-ethyl-benzothiazoline-6-sulfonic acid) (ABTS), oxygen radical absorbance capacity (ORAC), and thiobarbituric acid reactive substances using the in vitro and in vivo methods. RBPC at pH 7.0 presented a value of 95.80 μmoL TE/g of RBPC (FRAP); 257.12 μmoL TE/g of RBPC (ABTS), and 1960 μmoL TE/g of RBPC (ORAC). Duodenal digest of RBPC presented high antioxidant activity with 225.77 μmoL TE/g of digest (FRAP); 345.21 μmoL TE/g of digest (ABTS); and 3256 μmoL TE/g of digest (ORAC). Gastric and duodenal digest of RBPC were used to inhibit lipid peroxidation using the in vitro method presenting a value of 87.95% and 93.0%, respectively. When the in vivo method in zebrafish larvae was used, values were 79.03% and 86.76%, respectively. RBPCs showed no reactive oxygen species (ROS) inhibition. However, RBPCs with gastric and gastrointestinal digests, presented ROS inhibition, 75.30% for gastric digests and 66.40% for gastrointestinal digests.El concentrado de proteína de frijol rojo (RBPC) y sus hidrolizados se usaron para evaluar la capacidad antioxidante. El contenido de proteína RBPC estaba en el rango de 57.38% –72.68% del contenido total de la muestra. El perfil de proteína RBPC mostró un rango de 15 a 100 kDa. La proteína de faseolina se identificó con bandas de 45 y 50 kDa. Se encontró proteína de faseolina en todas las muestras de RBPC a los diferentes pH analizados. En la fase de digestión gástrica, las bandas de 60 a 100 kDa se hidrolizaron totalmente con pepsina. La proteína Phaseolin (45 y 50 kDa) presentó resistencia a la hidrólisis gástrica. Todos los RBPC y el digestivo gastrointestinal presentaron actividad antioxidante utilizando poder antioxidante reductor férrico (FRAP), 2,2-azinobis (ácido 3-etil-benzotiazolina-6-sulfónico) (ABTS), capacidad de absorbancia de radicales de oxígeno (ORAC) y tiobarbitúrico sustancias reactivas al ácido utilizando los métodos in vitro e in vivo. RBPC a pH 7.0 presentó un valor de 95.80 μmoL TE / g de RBPC (FRAP); 257.12 μmoL TE / g de RBPC (ABTS), y 1960 μmoL TE / g de RBPC (ORAC). La digestión duodenal de RBPC presentó una alta actividad antioxidante con 225.77 μmoL TE / g de digestión (FRAP); 345,21 μmoL TE / g de digestión (ABTS); y 3256 μmoL TE / g de digestión (ORAC). La digestión gástrica y duodenal de RBPC se utilizó para inhibir la peroxidación lipídica utilizando el método in vitro que presenta un valor de 87.95% y 93.0%, respectivamente. Cuando se usó el método in vivo en larvas de pez cebra, los valores fueron 79.03% y 86.76%, respectivamente. Las RBPC no mostraron inhibición de especies reactivas de oxígeno (ROS). Sin embargo, las RBPC con digestiones gástricas y gastrointestinales presentaron inhibición de ROS, 75.30% para las digeridas gástricas y 66.40% para las digeridas gastrointestinales.CrossMark2019-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfPiñuel, María L., Boeri, Patricia A., Vilcacundo, Edgar., Barrio, Daniel A., Morales, Dayana y et al. (2019). Extraction of protein concentrate from red bean (Phaseolus vulgaris L.): antioxidant activity and inhibition of lipid peroxidation. CrossMark; Journal of Applied Pharmaceutical Science; 9 (9); 45-58.2231-3354https://japsonline.com/abstract.php?article_id=2978https://rid.unrn.edu.ar/jspui/handle/20.500.12049/448010.7324/JAPS.2019.90804eng9 (9)Journal of Applied Pharmaceutical Scienceinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/4.0/reponame:RID-UNRN (UNRN)instname:Universidad Nacional de Río Negro2025-10-16T10:06:14Zoai:rid.unrn.edu.ar:20.500.12049/4480instacron:UNRNInstitucionalhttps://rid.unrn.edu.ar/jspui/Universidad públicaNo correspondehttps://rid.unrn.edu.ar/oai/snrdrid@unrn.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:43692025-10-16 10:06:14.485RID-UNRN (UNRN) - Universidad Nacional de Río Negrofalse |
dc.title.none.fl_str_mv |
Extraction of protein concentrate from red bean (Phaseolus vulgaris L.): antioxidant activity and inhibition of lipid peroxidation |
title |
Extraction of protein concentrate from red bean (Phaseolus vulgaris L.): antioxidant activity and inhibition of lipid peroxidation |
spellingShingle |
Extraction of protein concentrate from red bean (Phaseolus vulgaris L.): antioxidant activity and inhibition of lipid peroxidation Piñuel, María Lucrecia Common Bean Phaseolus Vulgaris Protein Concentrate Antioxidant Activity Zebrafish Larvae |
title_short |
Extraction of protein concentrate from red bean (Phaseolus vulgaris L.): antioxidant activity and inhibition of lipid peroxidation |
title_full |
Extraction of protein concentrate from red bean (Phaseolus vulgaris L.): antioxidant activity and inhibition of lipid peroxidation |
title_fullStr |
Extraction of protein concentrate from red bean (Phaseolus vulgaris L.): antioxidant activity and inhibition of lipid peroxidation |
title_full_unstemmed |
Extraction of protein concentrate from red bean (Phaseolus vulgaris L.): antioxidant activity and inhibition of lipid peroxidation |
title_sort |
Extraction of protein concentrate from red bean (Phaseolus vulgaris L.): antioxidant activity and inhibition of lipid peroxidation |
dc.creator.none.fl_str_mv |
Piñuel, María Lucrecia Vilcacundo, Edgar Boeri, Patricia Alejandra Barrio, Daniel Alejandro Morales, Dayana Pinto, Adelita Moran, Roberto Samaniego, Ivan Carrillo, Wilman |
author |
Piñuel, María Lucrecia |
author_facet |
Piñuel, María Lucrecia Vilcacundo, Edgar Boeri, Patricia Alejandra Barrio, Daniel Alejandro Morales, Dayana Pinto, Adelita Moran, Roberto Samaniego, Ivan Carrillo, Wilman |
author_role |
author |
author2 |
Vilcacundo, Edgar Boeri, Patricia Alejandra Barrio, Daniel Alejandro Morales, Dayana Pinto, Adelita Moran, Roberto Samaniego, Ivan Carrillo, Wilman |
author2_role |
author author author author author author author author |
dc.subject.none.fl_str_mv |
Common Bean Phaseolus Vulgaris Protein Concentrate Antioxidant Activity Zebrafish Larvae |
topic |
Common Bean Phaseolus Vulgaris Protein Concentrate Antioxidant Activity Zebrafish Larvae |
dc.description.none.fl_txt_mv |
Fil: Piñuel, María L. Universidad Nacional de Río Negro; Argentina Fil: Vilcacundo, Edgar. Bolivar State University. Department of Research; Ecuador. Fil: Boeri, Patricia A. Universidad Nacional de Río Negro; Argentina Fil: Barrio, Daniel A. Universidad Nacional de Río Negro; Argentina Fil: Morales, Dayana. Technical University of Ambato. Faculty of Science and Engineering in Food and Biotechnology; Ecuador. Fil: Pinto, Adelita. Technical University of Babahoyo. Department of Research; Ecuador. Fil: Moran, Roberto. National Institute of Agricultural Research (INIAP). Department of Nutrition and Quality; Ecuador. Fil: Samaniego, Ivan. National Institute of Agricultural Research (INIAP). Department of Nutrition and Quality; Ecuador. Fil: Carrillo, Wilman. Technical University of Babahoyo. Department of Research; Ecuador. Fil: Barrio, Daniel A. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Fil: Piñuel, María L. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Fil: Boeri, Patricia A. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Red Bean Protein Concentrate (RBPC) and their hydrolysates were used to evaluate the antioxidant capacity. The RBPC protein content was in the range of 57.38%–72.68% of the total sample content. RBPC protein profile showed a range of 15–100 kDa. Phaseolin protein was identified with bands of 45 and 50 kDa. Phaseolin protein was found in all the RBPC samples at the different pHs assayed. In the gastric digestion phase, bands from 60 to 100 kDa were totally hydrolyzed with pepsin. Phaseolin protein (45 and 50 kDa) presented resistance to gastric hydrolysis. All the RBPCs and gastrointestinal digest presented antioxidant activity using ferric-reducing antioxidant power (FRAP), 2,2-azinobis (3-ethyl-benzothiazoline-6-sulfonic acid) (ABTS), oxygen radical absorbance capacity (ORAC), and thiobarbituric acid reactive substances using the in vitro and in vivo methods. RBPC at pH 7.0 presented a value of 95.80 μmoL TE/g of RBPC (FRAP); 257.12 μmoL TE/g of RBPC (ABTS), and 1960 μmoL TE/g of RBPC (ORAC). Duodenal digest of RBPC presented high antioxidant activity with 225.77 μmoL TE/g of digest (FRAP); 345.21 μmoL TE/g of digest (ABTS); and 3256 μmoL TE/g of digest (ORAC). Gastric and duodenal digest of RBPC were used to inhibit lipid peroxidation using the in vitro method presenting a value of 87.95% and 93.0%, respectively. When the in vivo method in zebrafish larvae was used, values were 79.03% and 86.76%, respectively. RBPCs showed no reactive oxygen species (ROS) inhibition. However, RBPCs with gastric and gastrointestinal digests, presented ROS inhibition, 75.30% for gastric digests and 66.40% for gastrointestinal digests. El concentrado de proteína de frijol rojo (RBPC) y sus hidrolizados se usaron para evaluar la capacidad antioxidante. El contenido de proteína RBPC estaba en el rango de 57.38% –72.68% del contenido total de la muestra. El perfil de proteína RBPC mostró un rango de 15 a 100 kDa. La proteína de faseolina se identificó con bandas de 45 y 50 kDa. Se encontró proteína de faseolina en todas las muestras de RBPC a los diferentes pH analizados. En la fase de digestión gástrica, las bandas de 60 a 100 kDa se hidrolizaron totalmente con pepsina. La proteína Phaseolin (45 y 50 kDa) presentó resistencia a la hidrólisis gástrica. Todos los RBPC y el digestivo gastrointestinal presentaron actividad antioxidante utilizando poder antioxidante reductor férrico (FRAP), 2,2-azinobis (ácido 3-etil-benzotiazolina-6-sulfónico) (ABTS), capacidad de absorbancia de radicales de oxígeno (ORAC) y tiobarbitúrico sustancias reactivas al ácido utilizando los métodos in vitro e in vivo. RBPC a pH 7.0 presentó un valor de 95.80 μmoL TE / g de RBPC (FRAP); 257.12 μmoL TE / g de RBPC (ABTS), y 1960 μmoL TE / g de RBPC (ORAC). La digestión duodenal de RBPC presentó una alta actividad antioxidante con 225.77 μmoL TE / g de digestión (FRAP); 345,21 μmoL TE / g de digestión (ABTS); y 3256 μmoL TE / g de digestión (ORAC). La digestión gástrica y duodenal de RBPC se utilizó para inhibir la peroxidación lipídica utilizando el método in vitro que presenta un valor de 87.95% y 93.0%, respectivamente. Cuando se usó el método in vivo en larvas de pez cebra, los valores fueron 79.03% y 86.76%, respectivamente. Las RBPC no mostraron inhibición de especies reactivas de oxígeno (ROS). Sin embargo, las RBPC con digestiones gástricas y gastrointestinales presentaron inhibición de ROS, 75.30% para las digeridas gástricas y 66.40% para las digeridas gastrointestinales. |
description |
Fil: Piñuel, María L. Universidad Nacional de Río Negro; Argentina |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-09 |
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 |
Piñuel, María L., Boeri, Patricia A., Vilcacundo, Edgar., Barrio, Daniel A., Morales, Dayana y et al. (2019). Extraction of protein concentrate from red bean (Phaseolus vulgaris L.): antioxidant activity and inhibition of lipid peroxidation. CrossMark; Journal of Applied Pharmaceutical Science; 9 (9); 45-58. 2231-3354 https://japsonline.com/abstract.php?article_id=2978 https://rid.unrn.edu.ar/jspui/handle/20.500.12049/4480 10.7324/JAPS.2019.90804 |
identifier_str_mv |
Piñuel, María L., Boeri, Patricia A., Vilcacundo, Edgar., Barrio, Daniel A., Morales, Dayana y et al. (2019). Extraction of protein concentrate from red bean (Phaseolus vulgaris L.): antioxidant activity and inhibition of lipid peroxidation. CrossMark; Journal of Applied Pharmaceutical Science; 9 (9); 45-58. 2231-3354 10.7324/JAPS.2019.90804 |
url |
https://japsonline.com/abstract.php?article_id=2978 https://rid.unrn.edu.ar/jspui/handle/20.500.12049/4480 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
9 (9) Journal of Applied Pharmaceutical Science |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/4.0/ |
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openAccess |
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https://creativecommons.org/licenses/by-nc-sa/4.0/ |
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application/pdf |
dc.publisher.none.fl_str_mv |
CrossMark |
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CrossMark |
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reponame:RID-UNRN (UNRN) instname:Universidad Nacional de Río Negro |
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RID-UNRN (UNRN) |
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RID-UNRN (UNRN) |
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Universidad Nacional de Río Negro |
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RID-UNRN (UNRN) - Universidad Nacional de Río Negro |
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rid@unrn.edu.ar |
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