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

Autores
Bertucci, Juan Ignacio; Liggieri, Constanza Silvina; Colombo, María 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 ºC and pH 6.5. Proteolytic activity was 99% inactivated after 5 min of heat treatment (100 ºC). Major whey proteins degradation profile was analysed by tricine SDS-PAGE. After 180 min of hydrolysis alpha-lactalbumin (a- LA) and beta-lactoglobulin (b-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 reversedphase 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.
Centro de Investigación de Proteínas Vegetales
Materia
Biología
Plant peptidase
Maclura pomifera
Whey hydrolysate
Bioactive peptide
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-nd/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/191965
Acceder
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network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey proteinBertucci, Juan IgnacioLiggieri, Constanza SilvinaColombo, María LauraVairo Cavalli, Sandra ElizabethBruno, Mariela AnahíBiologíaPlant peptidaseMaclura pomiferaWhey hydrolysateBioactive peptideA 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 ºC and pH 6.5. Proteolytic activity was 99% inactivated after 5 min of heat treatment (100 ºC). Major whey proteins degradation profile was analysed by tricine SDS-PAGE. After 180 min of hydrolysis alpha-lactalbumin (a- LA) and beta-lactoglobulin (b-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 reversedphase 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.Centro de Investigación de Proteínas Vegetales2015info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf157-163http://sedici.unlp.edu.ar/handle/10915/191965enginfo:eu-repo/semantics/altIdentifier/issn/0023-6438info:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2015.05.041info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/4.0/Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2026-03-26T09:21:46Zoai:sedici.unlp.edu.ar:10915/191965Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292026-03-26 09:21:47.185SEDICI (UNLP) - Universidad Nacional de La Platafalse
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
Biología
Plant peptidase
Maclura pomifera
Whey hydrolysate
Bioactive peptide
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, María Laura
Vairo Cavalli, Sandra Elizabeth
Bruno, Mariela Anahí
author Bertucci, Juan Ignacio
author_facet Bertucci, Juan Ignacio
Liggieri, Constanza Silvina
Colombo, María Laura
Vairo Cavalli, Sandra Elizabeth
Bruno, Mariela Anahí
author_role author
author2 Liggieri, Constanza Silvina
Colombo, María Laura
Vairo Cavalli, Sandra Elizabeth
Bruno, Mariela Anahí
author2_role author
author
author
author
dc.subject.none.fl_str_mv Biología
Plant peptidase
Maclura pomifera
Whey hydrolysate
Bioactive peptide
topic Biología
Plant peptidase
Maclura pomifera
Whey hydrolysate
Bioactive peptide
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 ºC and pH 6.5. Proteolytic activity was 99% inactivated after 5 min of heat treatment (100 ºC). Major whey proteins degradation profile was analysed by tricine SDS-PAGE. After 180 min of hydrolysis alpha-lactalbumin (a- LA) and beta-lactoglobulin (b-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 reversedphase 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.
Centro de Investigación de Proteínas Vegetales
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 ºC and pH 6.5. Proteolytic activity was 99% inactivated after 5 min of heat treatment (100 ºC). Major whey proteins degradation profile was analysed by tricine SDS-PAGE. After 180 min of hydrolysis alpha-lactalbumin (a- LA) and beta-lactoglobulin (b-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 reversedphase 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
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/191965
url http://sedici.unlp.edu.ar/handle/10915/191965
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0023-6438
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2015.05.041
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-nd/4.0/
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/4.0/
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
dc.format.none.fl_str_mv application/pdf
157-163
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 12.977003

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