Potential antithrombotic activity detected in amaranth proteins and its hydrolysates
- Autores
- Sabbione, Ana Clara; Scilingo, Adriana Alicia; Añon, Maria Cristina
- Año de publicación
- 2014
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Amaranth protein isolate and fractions were obtained and subjected to proteolysis in order to evaluate its potential antithrombotic activity. The proteins were first hydrolyzed with alcalase (pH 10, 37 °C) and then with trypsin (pH 8, 37 °C). The samples were characterized physicochemically and antithrombotic activity was evaluated using clotting tests (PT, TT and APTT) and the microplates assay. The fractions compared to the hydrolysates exhibited different electrophoretic profiles (tricine-SDSPAGE) and gel filtration chromatograms, evidencing the presence of different molecular species. The hydrolysis improved in every sample the bioactivity detected, excepting for the glutelin fraction, which exhibited the highest antithrombotic activity, significantly superior (p < 0.05) compared to the other fractions and the isolate. This behavior was observed in the two assays that analyzed the common path of the coagulation cascade at similar concentrations: TT (81.0 ± 8.5 s with a control of 19.5 ± 0.7 s) and microplate test (IC50 80 μg/mL), indicating a possible mechanism of action that involves the thrombin activity or the polymerization of fibrin monomers. The glutelin fraction showed a potential capacity to inhibit coagulation, appearing as a promising ingredient to formulate functional foods.
Fil: Sabbione, Ana Clara. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina
Fil: Scilingo, Adriana Alicia. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina
Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina - Materia
-
Amaranth Proteins
Antithrombotic Activityx
Bioactive Peptides - 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:11336/33128
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Potential antithrombotic activity detected in amaranth proteins and its hydrolysatesSabbione, Ana ClaraScilingo, Adriana AliciaAñon, Maria CristinaAmaranth ProteinsAntithrombotic ActivityxBioactive Peptideshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Amaranth protein isolate and fractions were obtained and subjected to proteolysis in order to evaluate its potential antithrombotic activity. The proteins were first hydrolyzed with alcalase (pH 10, 37 °C) and then with trypsin (pH 8, 37 °C). The samples were characterized physicochemically and antithrombotic activity was evaluated using clotting tests (PT, TT and APTT) and the microplates assay. The fractions compared to the hydrolysates exhibited different electrophoretic profiles (tricine-SDSPAGE) and gel filtration chromatograms, evidencing the presence of different molecular species. The hydrolysis improved in every sample the bioactivity detected, excepting for the glutelin fraction, which exhibited the highest antithrombotic activity, significantly superior (p < 0.05) compared to the other fractions and the isolate. This behavior was observed in the two assays that analyzed the common path of the coagulation cascade at similar concentrations: TT (81.0 ± 8.5 s with a control of 19.5 ± 0.7 s) and microplate test (IC50 80 μg/mL), indicating a possible mechanism of action that involves the thrombin activity or the polymerization of fibrin monomers. The glutelin fraction showed a potential capacity to inhibit coagulation, appearing as a promising ingredient to formulate functional foods.Fil: Sabbione, Ana Clara. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; ArgentinaFil: Scilingo, Adriana Alicia. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; ArgentinaFil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; ArgentinaElsevier Science2014-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/33128Sabbione, Ana Clara; Scilingo, Adriana Alicia; Añon, Maria Cristina; Potential antithrombotic activity detected in amaranth proteins and its hydrolysates; Elsevier Science; LWT - Food Science and Technology; 60; 1; 7-2014; 171-1770023-6438CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2014.07.015info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0023643814004460info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:45:19Zoai:ri.conicet.gov.ar:11336/33128instacron: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:34982025-09-03 09:45:19.981CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Potential antithrombotic activity detected in amaranth proteins and its hydrolysates |
title |
Potential antithrombotic activity detected in amaranth proteins and its hydrolysates |
spellingShingle |
Potential antithrombotic activity detected in amaranth proteins and its hydrolysates Sabbione, Ana Clara Amaranth Proteins Antithrombotic Activityx Bioactive Peptides |
title_short |
Potential antithrombotic activity detected in amaranth proteins and its hydrolysates |
title_full |
Potential antithrombotic activity detected in amaranth proteins and its hydrolysates |
title_fullStr |
Potential antithrombotic activity detected in amaranth proteins and its hydrolysates |
title_full_unstemmed |
Potential antithrombotic activity detected in amaranth proteins and its hydrolysates |
title_sort |
Potential antithrombotic activity detected in amaranth proteins and its hydrolysates |
dc.creator.none.fl_str_mv |
Sabbione, Ana Clara Scilingo, Adriana Alicia Añon, Maria Cristina |
author |
Sabbione, Ana Clara |
author_facet |
Sabbione, Ana Clara Scilingo, Adriana Alicia Añon, Maria Cristina |
author_role |
author |
author2 |
Scilingo, Adriana Alicia Añon, Maria Cristina |
author2_role |
author author |
dc.subject.none.fl_str_mv |
Amaranth Proteins Antithrombotic Activityx Bioactive Peptides |
topic |
Amaranth Proteins Antithrombotic Activityx Bioactive Peptides |
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 isolate and fractions were obtained and subjected to proteolysis in order to evaluate its potential antithrombotic activity. The proteins were first hydrolyzed with alcalase (pH 10, 37 °C) and then with trypsin (pH 8, 37 °C). The samples were characterized physicochemically and antithrombotic activity was evaluated using clotting tests (PT, TT and APTT) and the microplates assay. The fractions compared to the hydrolysates exhibited different electrophoretic profiles (tricine-SDSPAGE) and gel filtration chromatograms, evidencing the presence of different molecular species. The hydrolysis improved in every sample the bioactivity detected, excepting for the glutelin fraction, which exhibited the highest antithrombotic activity, significantly superior (p < 0.05) compared to the other fractions and the isolate. This behavior was observed in the two assays that analyzed the common path of the coagulation cascade at similar concentrations: TT (81.0 ± 8.5 s with a control of 19.5 ± 0.7 s) and microplate test (IC50 80 μg/mL), indicating a possible mechanism of action that involves the thrombin activity or the polymerization of fibrin monomers. The glutelin fraction showed a potential capacity to inhibit coagulation, appearing as a promising ingredient to formulate functional foods. Fil: Sabbione, Ana Clara. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina Fil: Scilingo, Adriana Alicia. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina |
description |
Amaranth protein isolate and fractions were obtained and subjected to proteolysis in order to evaluate its potential antithrombotic activity. The proteins were first hydrolyzed with alcalase (pH 10, 37 °C) and then with trypsin (pH 8, 37 °C). The samples were characterized physicochemically and antithrombotic activity was evaluated using clotting tests (PT, TT and APTT) and the microplates assay. The fractions compared to the hydrolysates exhibited different electrophoretic profiles (tricine-SDSPAGE) and gel filtration chromatograms, evidencing the presence of different molecular species. The hydrolysis improved in every sample the bioactivity detected, excepting for the glutelin fraction, which exhibited the highest antithrombotic activity, significantly superior (p < 0.05) compared to the other fractions and the isolate. This behavior was observed in the two assays that analyzed the common path of the coagulation cascade at similar concentrations: TT (81.0 ± 8.5 s with a control of 19.5 ± 0.7 s) and microplate test (IC50 80 μg/mL), indicating a possible mechanism of action that involves the thrombin activity or the polymerization of fibrin monomers. The glutelin fraction showed a potential capacity to inhibit coagulation, appearing as a promising ingredient to formulate functional foods. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-07 |
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/11336/33128 Sabbione, Ana Clara; Scilingo, Adriana Alicia; Añon, Maria Cristina; Potential antithrombotic activity detected in amaranth proteins and its hydrolysates; Elsevier Science; LWT - Food Science and Technology; 60; 1; 7-2014; 171-177 0023-6438 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/33128 |
identifier_str_mv |
Sabbione, Ana Clara; Scilingo, Adriana Alicia; Añon, Maria Cristina; Potential antithrombotic activity detected in amaranth proteins and its hydrolysates; Elsevier Science; LWT - Food Science and Technology; 60; 1; 7-2014; 171-177 0023-6438 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2014.07.015 info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0023643814004460 |
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 application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier Science |
publisher.none.fl_str_mv |
Elsevier Science |
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) |
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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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1842268723505790976 |
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13.13397 |