ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex

Autores
Corrons, María Alicia; Liggieri, Constanza Silvina; Trejo, Sebastian Alejandro; Bruno, Mariela Anahí
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In work reported here, a proteolytic extract prepared from Maclura pomifera latex was employed to hydrolyze bovine caseins. Densitograms of Tricine–sodium-dodecyl-sulfate–polyacrylamide-gel electrophoresis (SDS-PAGE) indicated that the caseins were considerably degraded after a 10-min reaction. The degree of hydrolysis determined by the 2,4,6-trinitrobenzenesulfonic-acid method was 17.1���0.7% after 180�min of digestion. The concentration of small peptides increased with hydrolysis time, and analysis by reverse-phase high-performance liquid chromatography (RP HPLC) and mass spectrometry, revealed a virtually unchanged peptide profile. These results suggested that those proteases were highly specific, as only certain peptide bonds were cleaved. The hydrolysate of 180�min displayed the highest inhibition of angiotensin-converting enzyme (ACE) showing an IC50 of 1.72���0.25�mg/mL, and the analysis of the peptide fractionation in this hydrolysate by RP HPLC exhibited two peaks responsible for that activity. Fragmentation analysis through the use of iterated matrix-assisted–laser-desorption-ionization–time-of-flight mass spectrometry (MALDI-TOF/TOF MS/MS) with the aid of bioinformatics tools enabled us to deduce two peptide sequences—one, YQEPVLGPVRGPFPIIV, having been previously reported as an ACE-inhibitor; the other, RFFVAPFPE, as yet undescribed. The presence of bioactive peptides in these casein hydrolysates argues for their potential use in the development of functional foods.
Fil: Corrons, María Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Liggieri, Constanza Silvina. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Trejo, Sebastian Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina
Fil: Bruno, Mariela Anahí. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Materia
Ace-Inhibitory Peptide
Hydrolysate
Maclura Pomifera
Plant Peptidase
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/49568
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/49568
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latexCorrons, María AliciaLiggieri, Constanza SilvinaTrejo, Sebastian AlejandroBruno, Mariela AnahíAce-Inhibitory PeptideHydrolysateMaclura PomiferaPlant Peptidasehttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2In work reported here, a proteolytic extract prepared from Maclura pomifera latex was employed to hydrolyze bovine caseins. Densitograms of Tricine–sodium-dodecyl-sulfate–polyacrylamide-gel electrophoresis (SDS-PAGE) indicated that the caseins were considerably degraded after a 10-min reaction. The degree of hydrolysis determined by the 2,4,6-trinitrobenzenesulfonic-acid method was 17.1���0.7% after 180�min of digestion. The concentration of small peptides increased with hydrolysis time, and analysis by reverse-phase high-performance liquid chromatography (RP HPLC) and mass spectrometry, revealed a virtually unchanged peptide profile. These results suggested that those proteases were highly specific, as only certain peptide bonds were cleaved. The hydrolysate of 180�min displayed the highest inhibition of angiotensin-converting enzyme (ACE) showing an IC50 of 1.72���0.25�mg/mL, and the analysis of the peptide fractionation in this hydrolysate by RP HPLC exhibited two peaks responsible for that activity. Fragmentation analysis through the use of iterated matrix-assisted–laser-desorption-ionization–time-of-flight mass spectrometry (MALDI-TOF/TOF MS/MS) with the aid of bioinformatics tools enabled us to deduce two peptide sequences—one, YQEPVLGPVRGPFPIIV, having been previously reported as an ACE-inhibitor; the other, RFFVAPFPE, as yet undescribed. The presence of bioactive peptides in these casein hydrolysates argues for their potential use in the development of functional foods.Fil: Corrons, María Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; ArgentinaFil: Liggieri, Constanza Silvina. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; ArgentinaFil: Trejo, Sebastian Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; ArgentinaFil: Bruno, Mariela Anahí. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; ArgentinaElsevier Science2017-03info: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/11336/49568Corrons, María Alicia; Liggieri, Constanza Silvina; Trejo, Sebastian Alejandro; Bruno, Mariela Anahí; ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex; Elsevier Science; Food Research International; 93; 3-2017; 8-150963-9969CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2017.01.003info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0963996917300042info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:03:09Zoai:ri.conicet.gov.ar:11336/49568instacron: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:34982025-10-22 11:03:09.675CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex
title ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex
spellingShingle ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex
Corrons, María Alicia
Ace-Inhibitory Peptide
Hydrolysate
Maclura Pomifera
Plant Peptidase
title_short ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex
title_full ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex
title_fullStr ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex
title_full_unstemmed ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex
title_sort ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex
dc.creator.none.fl_str_mv Corrons, María Alicia
Liggieri, Constanza Silvina
Trejo, Sebastian Alejandro
Bruno, Mariela Anahí
author Corrons, María Alicia
author_facet Corrons, María Alicia
Liggieri, Constanza Silvina
Trejo, Sebastian Alejandro
Bruno, Mariela Anahí
author_role author
author2 Liggieri, Constanza Silvina
Trejo, Sebastian Alejandro
Bruno, Mariela Anahí
author2_role author
author
author
dc.subject.none.fl_str_mv Ace-Inhibitory Peptide
Hydrolysate
Maclura Pomifera
Plant Peptidase
topic Ace-Inhibitory Peptide
Hydrolysate
Maclura Pomifera
Plant Peptidase
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv In work reported here, a proteolytic extract prepared from Maclura pomifera latex was employed to hydrolyze bovine caseins. Densitograms of Tricine–sodium-dodecyl-sulfate–polyacrylamide-gel electrophoresis (SDS-PAGE) indicated that the caseins were considerably degraded after a 10-min reaction. The degree of hydrolysis determined by the 2,4,6-trinitrobenzenesulfonic-acid method was 17.1���0.7% after 180�min of digestion. The concentration of small peptides increased with hydrolysis time, and analysis by reverse-phase high-performance liquid chromatography (RP HPLC) and mass spectrometry, revealed a virtually unchanged peptide profile. These results suggested that those proteases were highly specific, as only certain peptide bonds were cleaved. The hydrolysate of 180�min displayed the highest inhibition of angiotensin-converting enzyme (ACE) showing an IC50 of 1.72���0.25�mg/mL, and the analysis of the peptide fractionation in this hydrolysate by RP HPLC exhibited two peaks responsible for that activity. Fragmentation analysis through the use of iterated matrix-assisted–laser-desorption-ionization–time-of-flight mass spectrometry (MALDI-TOF/TOF MS/MS) with the aid of bioinformatics tools enabled us to deduce two peptide sequences—one, YQEPVLGPVRGPFPIIV, having been previously reported as an ACE-inhibitor; the other, RFFVAPFPE, as yet undescribed. The presence of bioactive peptides in these casein hydrolysates argues for their potential use in the development of functional foods.
Fil: Corrons, María Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Liggieri, Constanza Silvina. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Trejo, Sebastian Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina
Fil: Bruno, Mariela Anahí. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
description In work reported here, a proteolytic extract prepared from Maclura pomifera latex was employed to hydrolyze bovine caseins. Densitograms of Tricine–sodium-dodecyl-sulfate–polyacrylamide-gel electrophoresis (SDS-PAGE) indicated that the caseins were considerably degraded after a 10-min reaction. The degree of hydrolysis determined by the 2,4,6-trinitrobenzenesulfonic-acid method was 17.1���0.7% after 180�min of digestion. The concentration of small peptides increased with hydrolysis time, and analysis by reverse-phase high-performance liquid chromatography (RP HPLC) and mass spectrometry, revealed a virtually unchanged peptide profile. These results suggested that those proteases were highly specific, as only certain peptide bonds were cleaved. The hydrolysate of 180�min displayed the highest inhibition of angiotensin-converting enzyme (ACE) showing an IC50 of 1.72���0.25�mg/mL, and the analysis of the peptide fractionation in this hydrolysate by RP HPLC exhibited two peaks responsible for that activity. Fragmentation analysis through the use of iterated matrix-assisted–laser-desorption-ionization–time-of-flight mass spectrometry (MALDI-TOF/TOF MS/MS) with the aid of bioinformatics tools enabled us to deduce two peptide sequences—one, YQEPVLGPVRGPFPIIV, having been previously reported as an ACE-inhibitor; the other, RFFVAPFPE, as yet undescribed. The presence of bioactive peptides in these casein hydrolysates argues for their potential use in the development of functional foods.
publishDate 2017
dc.date.none.fl_str_mv 2017-03
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/11336/49568
Corrons, María Alicia; Liggieri, Constanza Silvina; Trejo, Sebastian Alejandro; Bruno, Mariela Anahí; ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex; Elsevier Science; Food Research International; 93; 3-2017; 8-15
0963-9969
CONICET Digital
CONICET
url http://hdl.handle.net/11336/49568
identifier_str_mv Corrons, María Alicia; Liggieri, Constanza Silvina; Trejo, Sebastian Alejandro; Bruno, Mariela Anahí; ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex; Elsevier Science; Food Research International; 93; 3-2017; 8-15
0963-9969
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.foodres.2017.01.003
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0963996917300042
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/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)
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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