Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey protein

Autores
Bertucci, Juan Ignacio; Liggieri, Constanza Silvina; Colombo, Maria Laura; Vairo Cavalli, Sandra Elizabeth; Bruno, Mariela Anahí
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A crude extract containing serine peptidases, was prepared from latex of Maclura pomifera fruits. Peptidases were isolated by precipitation with one volume of ethanol with a yield of 5.4 ± 0.4 Ucas per milligram of protein. This extract was used for hydrolysis of bovine whey proteins at 45 °C and pH 6.5. Proteolytic activity was 99% inactivated after 5 min of heat treatment (100 °C). Major whey proteins degradation profile was analysed by tricine SDS-PAGE. After 180 min of hydrolysis alpha-lactalbumin (α-LA) and beta-lactoglobulin (β-LG) were almost completely degraded. Hydrolysis degree was 31.3 ± 1.7% at 180 min of reaction and the peptides produced that were smaller than 3 kDa were analysed by reversed-phase high-performance liquid chromatography (RP-HPLC). Angiotensin-converting enzyme (ACE) inhibitory activity and antioxidant capacity were detected in the hydrolysates and IC50 values for 180 min of hydrolysis were 0.53 ± 0.02 and 4.44 ± 0.44 mg/ml, respectively. One peptide sequence deduced from peptide masses in the 180 min filtered hydrolysate, coincided with an ACE-inhibitory peptide reported by other author. The results support the conclusion that, by the presence of ACE-inhibitory and antioxidant peptides, it would be possible to use these whey protein hydrolysates for functional food manufacturing.
Fil: Bertucci, Juan Ignacio. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Liggieri, Constanza Silvina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Colombo, Maria Laura. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Bruno, Mariela Anahí. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Bioactive Peptide
Maclura Pomifera
Plant Peptidase
Whey Hydrolysate
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:11336/53698
Acceder
id CONICETDig_53c199a124bfc7b0c57178dfd65c9077
oai_identifier_str oai:ri.conicet.gov.ar:11336/53698
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey proteinBertucci, Juan IgnacioLiggieri, Constanza SilvinaColombo, Maria LauraVairo Cavalli, Sandra ElizabethBruno, Mariela AnahíBioactive PeptideMaclura PomiferaPlant PeptidaseWhey HydrolysateA crude extract containing serine peptidases, was prepared from latex of Maclura pomifera fruits. Peptidases were isolated by precipitation with one volume of ethanol with a yield of 5.4 ± 0.4 Ucas per milligram of protein. This extract was used for hydrolysis of bovine whey proteins at 45 °C and pH 6.5. Proteolytic activity was 99% inactivated after 5 min of heat treatment (100 °C). Major whey proteins degradation profile was analysed by tricine SDS-PAGE. After 180 min of hydrolysis alpha-lactalbumin (α-LA) and beta-lactoglobulin (β-LG) were almost completely degraded. Hydrolysis degree was 31.3 ± 1.7% at 180 min of reaction and the peptides produced that were smaller than 3 kDa were analysed by reversed-phase high-performance liquid chromatography (RP-HPLC). Angiotensin-converting enzyme (ACE) inhibitory activity and antioxidant capacity were detected in the hydrolysates and IC50 values for 180 min of hydrolysis were 0.53 ± 0.02 and 4.44 ± 0.44 mg/ml, respectively. One peptide sequence deduced from peptide masses in the 180 min filtered hydrolysate, coincided with an ACE-inhibitory peptide reported by other author. The results support the conclusion that, by the presence of ACE-inhibitory and antioxidant peptides, it would be possible to use these whey protein hydrolysates for functional food manufacturing.Fil: Bertucci, Juan Ignacio. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Liggieri, Constanza Silvina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Colombo, Maria Laura. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Bruno, Mariela Anahí. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier Science2015-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/53698Bertucci, Juan Ignacio; Liggieri, Constanza Silvina; Colombo, Maria Laura; Vairo Cavalli, Sandra Elizabeth; Bruno, Mariela Anahí; Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey protein; Elsevier Science; LWT - Food Science and Technology; 64; 1; 11-2015; 157-1630023-6438CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2015.05.041info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0023643815004041info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:55:49Zoai:ri.conicet.gov.ar:11336/53698instacron: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 09:55:50.019CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey protein
title Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey protein
spellingShingle Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey protein
Bertucci, Juan Ignacio
Bioactive Peptide
Maclura Pomifera
Plant Peptidase
Whey Hydrolysate
title_short Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey protein
title_full Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey protein
title_fullStr Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey protein
title_full_unstemmed Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey protein
title_sort Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey protein
dc.creator.none.fl_str_mv Bertucci, Juan Ignacio
Liggieri, Constanza Silvina
Colombo, Maria Laura
Vairo Cavalli, Sandra Elizabeth
Bruno, Mariela Anahí
author Bertucci, Juan Ignacio
author_facet Bertucci, Juan Ignacio
Liggieri, Constanza Silvina
Colombo, Maria Laura
Vairo Cavalli, Sandra Elizabeth
Bruno, Mariela Anahí
author_role author
author2 Liggieri, Constanza Silvina
Colombo, Maria Laura
Vairo Cavalli, Sandra Elizabeth
Bruno, Mariela Anahí
author2_role author
author
author
author
dc.subject.none.fl_str_mv Bioactive Peptide
Maclura Pomifera
Plant Peptidase
Whey Hydrolysate
topic Bioactive Peptide
Maclura Pomifera
Plant Peptidase
Whey Hydrolysate
dc.description.none.fl_txt_mv A crude extract containing serine peptidases, was prepared from latex of Maclura pomifera fruits. Peptidases were isolated by precipitation with one volume of ethanol with a yield of 5.4 ± 0.4 Ucas per milligram of protein. This extract was used for hydrolysis of bovine whey proteins at 45 °C and pH 6.5. Proteolytic activity was 99% inactivated after 5 min of heat treatment (100 °C). Major whey proteins degradation profile was analysed by tricine SDS-PAGE. After 180 min of hydrolysis alpha-lactalbumin (α-LA) and beta-lactoglobulin (β-LG) were almost completely degraded. Hydrolysis degree was 31.3 ± 1.7% at 180 min of reaction and the peptides produced that were smaller than 3 kDa were analysed by reversed-phase high-performance liquid chromatography (RP-HPLC). Angiotensin-converting enzyme (ACE) inhibitory activity and antioxidant capacity were detected in the hydrolysates and IC50 values for 180 min of hydrolysis were 0.53 ± 0.02 and 4.44 ± 0.44 mg/ml, respectively. One peptide sequence deduced from peptide masses in the 180 min filtered hydrolysate, coincided with an ACE-inhibitory peptide reported by other author. The results support the conclusion that, by the presence of ACE-inhibitory and antioxidant peptides, it would be possible to use these whey protein hydrolysates for functional food manufacturing.
Fil: Bertucci, Juan Ignacio. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Liggieri, Constanza Silvina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Colombo, Maria Laura. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Bruno, Mariela Anahí. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description A crude extract containing serine peptidases, was prepared from latex of Maclura pomifera fruits. Peptidases were isolated by precipitation with one volume of ethanol with a yield of 5.4 ± 0.4 Ucas per milligram of protein. This extract was used for hydrolysis of bovine whey proteins at 45 °C and pH 6.5. Proteolytic activity was 99% inactivated after 5 min of heat treatment (100 °C). Major whey proteins degradation profile was analysed by tricine SDS-PAGE. After 180 min of hydrolysis alpha-lactalbumin (α-LA) and beta-lactoglobulin (β-LG) were almost completely degraded. Hydrolysis degree was 31.3 ± 1.7% at 180 min of reaction and the peptides produced that were smaller than 3 kDa were analysed by reversed-phase high-performance liquid chromatography (RP-HPLC). Angiotensin-converting enzyme (ACE) inhibitory activity and antioxidant capacity were detected in the hydrolysates and IC50 values for 180 min of hydrolysis were 0.53 ± 0.02 and 4.44 ± 0.44 mg/ml, respectively. One peptide sequence deduced from peptide masses in the 180 min filtered hydrolysate, coincided with an ACE-inhibitory peptide reported by other author. The results support the conclusion that, by the presence of ACE-inhibitory and antioxidant peptides, it would be possible to use these whey protein hydrolysates for functional food manufacturing.
publishDate 2015
dc.date.none.fl_str_mv 2015-11
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/11336/53698
Bertucci, Juan Ignacio; Liggieri, Constanza Silvina; Colombo, Maria Laura; Vairo Cavalli, Sandra Elizabeth; Bruno, Mariela Anahí; Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey protein; Elsevier Science; LWT - Food Science and Technology; 64; 1; 11-2015; 157-163
0023-6438
CONICET Digital
CONICET
url http://hdl.handle.net/11336/53698
identifier_str_mv Bertucci, Juan Ignacio; Liggieri, Constanza Silvina; Colombo, Maria Laura; Vairo Cavalli, Sandra Elizabeth; Bruno, Mariela Anahí; Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey protein; Elsevier Science; LWT - Food Science and Technology; 64; 1; 11-2015; 157-163
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.2015.05.041
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0023643815004041
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
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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score 13.13397

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