Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus

Autores
Castellano, Patricia Haydee; Aristoy, María Concepción; Sentandreu, Miguel Ángel; Vignolo, Graciela Margarita; Toldrá, Fidel
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Angiotensin I-converting enzyme (ACE) inhibitory activity of peptides derived from the hydrolysis of sarcoplasmic and myofibrillar porcine proteins by the action of Lactobacillus sakei CRL1862 and Lactobacillus curvatus CRL705 (whole cells + cell free extracts) was investigated at 30 °C for 36 h. The protein hydrolysates were subjected to RP-HPLC in order to fractionate the extracts for further evaluate the ACE inhibitory activity of the collected peptide fractions. Bioactive fractions were only found from the hydrolysis of sarcoplasmic proteins by both assayed lactic acid bacteria. Identification of peptides contained in these bioactive fractions was carried out by tandem mass spectrometry using a nanoLC-ESI-QTOF instrument and the mascot seach engine. A total of eighteen peptides were characterized from the two most active fractions obtained from the hydrolysis made by L. sakei CRL1862. Regarding L. curvatus CRL705, its proteolytic action was able to generate thirty and twenty peptides, which were identified in the two most active fractions, respectively. It is worth noting that the sequence FISNHAY was generated by the proteolytic action of the two species. Sequence similarity analyses between the peptides identified in this study and those previously identified as ACE inhibitory peptides and detailed in the BIOPEP database were outlined. Results suggest that lactic acid bacteria selected in this study were able to generate peptides with ACE inhibitory activity, thus having potential to be used in the development of functional fermented products.
Fil: Castellano, Patricia Haydee. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Centro de Referencia para Lactobacilos (i); Argentina
Fil: Aristoy, María Concepción. Consejo Superior de Investigaciones Cientificas. Instituto de Ciencia y Teconologia de Alimentos y Nutricion; España;
Fil: Sentandreu, Miguel Ángel. Consejo Superior de Investigaciones Cientificas. Instituto de Ciencia y Teconologia de Alimentos y Nutricion; España;
Fil: Vignolo, Graciela Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Centro de Referencia para Lactobacilos (i); Argentina
Fil: Toldrá, Fidel. Consejo Superior de Investigaciones Cientificas. Instituto de Ciencia y Teconologia de Alimentos y Nutricion; España;
Materia
Proteomics
Bioactive Peptides
Angiotensin I-Converting Enzyme
Meat Products
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/2203
Acceder
id CONICETDig_3bf25881feda3bdb749edb554431c9e2
oai_identifier_str oai:ri.conicet.gov.ar:11336/2203
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne LactobacillusCastellano, Patricia HaydeeAristoy, María ConcepciónSentandreu, Miguel ÁngelVignolo, Graciela MargaritaToldrá, FidelProteomicsBioactive PeptidesAngiotensin I-Converting EnzymeMeat Productshttps://purl.org/becyt/ford/3.4https://purl.org/becyt/ford/3Angiotensin I-converting enzyme (ACE) inhibitory activity of peptides derived from the hydrolysis of sarcoplasmic and myofibrillar porcine proteins by the action of Lactobacillus sakei CRL1862 and Lactobacillus curvatus CRL705 (whole cells + cell free extracts) was investigated at 30 °C for 36 h. The protein hydrolysates were subjected to RP-HPLC in order to fractionate the extracts for further evaluate the ACE inhibitory activity of the collected peptide fractions. Bioactive fractions were only found from the hydrolysis of sarcoplasmic proteins by both assayed lactic acid bacteria. Identification of peptides contained in these bioactive fractions was carried out by tandem mass spectrometry using a nanoLC-ESI-QTOF instrument and the mascot seach engine. A total of eighteen peptides were characterized from the two most active fractions obtained from the hydrolysis made by L. sakei CRL1862. Regarding L. curvatus CRL705, its proteolytic action was able to generate thirty and twenty peptides, which were identified in the two most active fractions, respectively. It is worth noting that the sequence FISNHAY was generated by the proteolytic action of the two species. Sequence similarity analyses between the peptides identified in this study and those previously identified as ACE inhibitory peptides and detailed in the BIOPEP database were outlined. Results suggest that lactic acid bacteria selected in this study were able to generate peptides with ACE inhibitory activity, thus having potential to be used in the development of functional fermented products.Fil: Castellano, Patricia Haydee. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Centro de Referencia para Lactobacilos (i); ArgentinaFil: Aristoy, María Concepción. Consejo Superior de Investigaciones Cientificas. Instituto de Ciencia y Teconologia de Alimentos y Nutricion; España;Fil: Sentandreu, Miguel Ángel. Consejo Superior de Investigaciones Cientificas. Instituto de Ciencia y Teconologia de Alimentos y Nutricion; España;Fil: Vignolo, Graciela Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Centro de Referencia para Lactobacilos (i); ArgentinaFil: Toldrá, Fidel. Consejo Superior de Investigaciones Cientificas. Instituto de Ciencia y Teconologia de Alimentos y Nutricion; España;Elsevier Science2013-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/2203Castellano, Patricia Haydee; Aristoy, María Concepción; Sentandreu, Miguel Ángel; Vignolo, Graciela Margarita; Toldrá, Fidel; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus; Elsevier Science; Journal Of Proteomics; 89; 8-2013; 183-1901874-3919enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1874391913003497info:eu-repo/semantics/altIdentifier/url/http://www.ncbi.nlm.nih.gov/pubmed/23806758info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:09:04Zoai:ri.conicet.gov.ar:11336/2203instacron: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 10:09:04.681CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus
title Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus
spellingShingle Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus
Castellano, Patricia Haydee
Proteomics
Bioactive Peptides
Angiotensin I-Converting Enzyme
Meat Products
title_short Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus
title_full Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus
title_fullStr Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus
title_full_unstemmed Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus
title_sort Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus
dc.creator.none.fl_str_mv Castellano, Patricia Haydee
Aristoy, María Concepción
Sentandreu, Miguel Ángel
Vignolo, Graciela Margarita
Toldrá, Fidel
author Castellano, Patricia Haydee
author_facet Castellano, Patricia Haydee
Aristoy, María Concepción
Sentandreu, Miguel Ángel
Vignolo, Graciela Margarita
Toldrá, Fidel
author_role author
author2 Aristoy, María Concepción
Sentandreu, Miguel Ángel
Vignolo, Graciela Margarita
Toldrá, Fidel
author2_role author
author
author
author
dc.subject.none.fl_str_mv Proteomics
Bioactive Peptides
Angiotensin I-Converting Enzyme
Meat Products
topic Proteomics
Bioactive Peptides
Angiotensin I-Converting Enzyme
Meat Products
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.4
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Angiotensin I-converting enzyme (ACE) inhibitory activity of peptides derived from the hydrolysis of sarcoplasmic and myofibrillar porcine proteins by the action of Lactobacillus sakei CRL1862 and Lactobacillus curvatus CRL705 (whole cells + cell free extracts) was investigated at 30 °C for 36 h. The protein hydrolysates were subjected to RP-HPLC in order to fractionate the extracts for further evaluate the ACE inhibitory activity of the collected peptide fractions. Bioactive fractions were only found from the hydrolysis of sarcoplasmic proteins by both assayed lactic acid bacteria. Identification of peptides contained in these bioactive fractions was carried out by tandem mass spectrometry using a nanoLC-ESI-QTOF instrument and the mascot seach engine. A total of eighteen peptides were characterized from the two most active fractions obtained from the hydrolysis made by L. sakei CRL1862. Regarding L. curvatus CRL705, its proteolytic action was able to generate thirty and twenty peptides, which were identified in the two most active fractions, respectively. It is worth noting that the sequence FISNHAY was generated by the proteolytic action of the two species. Sequence similarity analyses between the peptides identified in this study and those previously identified as ACE inhibitory peptides and detailed in the BIOPEP database were outlined. Results suggest that lactic acid bacteria selected in this study were able to generate peptides with ACE inhibitory activity, thus having potential to be used in the development of functional fermented products.
Fil: Castellano, Patricia Haydee. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Centro de Referencia para Lactobacilos (i); Argentina
Fil: Aristoy, María Concepción. Consejo Superior de Investigaciones Cientificas. Instituto de Ciencia y Teconologia de Alimentos y Nutricion; España;
Fil: Sentandreu, Miguel Ángel. Consejo Superior de Investigaciones Cientificas. Instituto de Ciencia y Teconologia de Alimentos y Nutricion; España;
Fil: Vignolo, Graciela Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Centro de Referencia para Lactobacilos (i); Argentina
Fil: Toldrá, Fidel. Consejo Superior de Investigaciones Cientificas. Instituto de Ciencia y Teconologia de Alimentos y Nutricion; España;
description Angiotensin I-converting enzyme (ACE) inhibitory activity of peptides derived from the hydrolysis of sarcoplasmic and myofibrillar porcine proteins by the action of Lactobacillus sakei CRL1862 and Lactobacillus curvatus CRL705 (whole cells + cell free extracts) was investigated at 30 °C for 36 h. The protein hydrolysates were subjected to RP-HPLC in order to fractionate the extracts for further evaluate the ACE inhibitory activity of the collected peptide fractions. Bioactive fractions were only found from the hydrolysis of sarcoplasmic proteins by both assayed lactic acid bacteria. Identification of peptides contained in these bioactive fractions was carried out by tandem mass spectrometry using a nanoLC-ESI-QTOF instrument and the mascot seach engine. A total of eighteen peptides were characterized from the two most active fractions obtained from the hydrolysis made by L. sakei CRL1862. Regarding L. curvatus CRL705, its proteolytic action was able to generate thirty and twenty peptides, which were identified in the two most active fractions, respectively. It is worth noting that the sequence FISNHAY was generated by the proteolytic action of the two species. Sequence similarity analyses between the peptides identified in this study and those previously identified as ACE inhibitory peptides and detailed in the BIOPEP database were outlined. Results suggest that lactic acid bacteria selected in this study were able to generate peptides with ACE inhibitory activity, thus having potential to be used in the development of functional fermented products.
publishDate 2013
dc.date.none.fl_str_mv 2013-08
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/11336/2203
Castellano, Patricia Haydee; Aristoy, María Concepción; Sentandreu, Miguel Ángel; Vignolo, Graciela Margarita; Toldrá, Fidel; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus; Elsevier Science; Journal Of Proteomics; 89; 8-2013; 183-190
1874-3919
url http://hdl.handle.net/11336/2203
identifier_str_mv Castellano, Patricia Haydee; Aristoy, María Concepción; Sentandreu, Miguel Ángel; Vignolo, Graciela Margarita; Toldrá, Fidel; Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus; Elsevier Science; Journal Of Proteomics; 89; 8-2013; 183-190
1874-3919
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1874391913003497
info:eu-repo/semantics/altIdentifier/url/http://www.ncbi.nlm.nih.gov/pubmed/23806758
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
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
_version_ 1842270068145127424
score 13.13397

Publicaciones similares