Preparation of soy protein hydrolysates with antioxidant activity by using peptidases from latex of Maclura pomifera fruits

Autores
Reyes Jara, Andrea Milagros; Liggieri, Constanza Silvina; Bruno, Mariela Anahí
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A partially purified proteolytic extract prepared from Maclura pomifera latex was employed in hydrolyzing a soybean-protein isolate (4.2 mg/mL). The hydrolysis-product formation, monitored by tricine–sodium-dodecyl-sulfate–polyacrylamyde-gel electrophoresis and reverse-phase high-performance liquid chromatography, indicated that after 10 min of reaction the main soybean proteins disappeared. The maximum degree of hydrolysis was 36.2% after a 180-min digestion. The 90-min hydrolysate presented an IC50 of 31.6 ± 0.2 µg/mL, and a trolox equivalent antioxidant capacity of 157.6 and 176.9 µmoles TE per g of peptide determined by two different methods. Analysis by matrix-assisted–laser-desorption-ionization–time-of-flight mass spectrometry (MALDI-TOF MS), followed by the application of bioinformatics tools, enabled the deduction of fourteen theoretical peptide sequences containing antioxidant amino acids at >60%, none of which sequences had been previously reported as antioxidants. Finally, we consider that this 90-min hydrolysate would constitute a promising ingredient in the manufacture of functional foods.
Instituto de Fisiología Vegetal
Centro de Investigación de Proteínas Vegetales
Materia
Biología
Maclura pomifera
Plant peptidases
Soybean-protein isolate
Protein hydrolysate
Bioactive peptide
Antioxidant activity
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/127934

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oai_identifier_str oai:sedici.unlp.edu.ar:10915/127934
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Preparation of soy protein hydrolysates with antioxidant activity by using peptidases from latex of Maclura pomifera fruitsReyes Jara, Andrea MilagrosLiggieri, Constanza SilvinaBruno, Mariela AnahíBiologíaMaclura pomiferaPlant peptidasesSoybean-protein isolateProtein hydrolysateBioactive peptideAntioxidant activityA partially purified proteolytic extract prepared from Maclura pomifera latex was employed in hydrolyzing a soybean-protein isolate (4.2 mg/mL). The hydrolysis-product formation, monitored by tricine–sodium-dodecyl-sulfate–polyacrylamyde-gel electrophoresis and reverse-phase high-performance liquid chromatography, indicated that after 10 min of reaction the main soybean proteins disappeared. The maximum degree of hydrolysis was 36.2% after a 180-min digestion. The 90-min hydrolysate presented an IC50 of 31.6 ± 0.2 µg/mL, and a trolox equivalent antioxidant capacity of 157.6 and 176.9 µmoles TE per g of peptide determined by two different methods. Analysis by matrix-assisted–laser-desorption-ionization–time-of-flight mass spectrometry (MALDI-TOF MS), followed by the application of bioinformatics tools, enabled the deduction of fourteen theoretical peptide sequences containing antioxidant amino acids at >60%, none of which sequences had been previously reported as antioxidants. Finally, we consider that this 90-min hydrolysate would constitute a promising ingredient in the manufacture of functional foods.Instituto de Fisiología VegetalCentro de Investigación de Proteínas Vegetales2018-05-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf326-333http://sedici.unlp.edu.ar/handle/10915/127934enginfo:eu-repo/semantics/altIdentifier/issn/1873-7072info:eu-repo/semantics/altIdentifier/issn/0308-8146info:eu-repo/semantics/altIdentifier/pmid/29853383info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodchem.2018.05.013info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:30:58Zoai:sedici.unlp.edu.ar:10915/127934Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:30:59.0SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Preparation of soy protein hydrolysates with antioxidant activity by using peptidases from latex of Maclura pomifera fruits
title Preparation of soy protein hydrolysates with antioxidant activity by using peptidases from latex of Maclura pomifera fruits
spellingShingle Preparation of soy protein hydrolysates with antioxidant activity by using peptidases from latex of Maclura pomifera fruits
Reyes Jara, Andrea Milagros
Biología
Maclura pomifera
Plant peptidases
Soybean-protein isolate
Protein hydrolysate
Bioactive peptide
Antioxidant activity
title_short Preparation of soy protein hydrolysates with antioxidant activity by using peptidases from latex of Maclura pomifera fruits
title_full Preparation of soy protein hydrolysates with antioxidant activity by using peptidases from latex of Maclura pomifera fruits
title_fullStr Preparation of soy protein hydrolysates with antioxidant activity by using peptidases from latex of Maclura pomifera fruits
title_full_unstemmed Preparation of soy protein hydrolysates with antioxidant activity by using peptidases from latex of Maclura pomifera fruits
title_sort Preparation of soy protein hydrolysates with antioxidant activity by using peptidases from latex of Maclura pomifera fruits
dc.creator.none.fl_str_mv Reyes Jara, Andrea Milagros
Liggieri, Constanza Silvina
Bruno, Mariela Anahí
author Reyes Jara, Andrea Milagros
author_facet Reyes Jara, Andrea Milagros
Liggieri, Constanza Silvina
Bruno, Mariela Anahí
author_role author
author2 Liggieri, Constanza Silvina
Bruno, Mariela Anahí
author2_role author
author
dc.subject.none.fl_str_mv Biología
Maclura pomifera
Plant peptidases
Soybean-protein isolate
Protein hydrolysate
Bioactive peptide
Antioxidant activity
topic Biología
Maclura pomifera
Plant peptidases
Soybean-protein isolate
Protein hydrolysate
Bioactive peptide
Antioxidant activity
dc.description.none.fl_txt_mv A partially purified proteolytic extract prepared from Maclura pomifera latex was employed in hydrolyzing a soybean-protein isolate (4.2 mg/mL). The hydrolysis-product formation, monitored by tricine–sodium-dodecyl-sulfate–polyacrylamyde-gel electrophoresis and reverse-phase high-performance liquid chromatography, indicated that after 10 min of reaction the main soybean proteins disappeared. The maximum degree of hydrolysis was 36.2% after a 180-min digestion. The 90-min hydrolysate presented an IC50 of 31.6 ± 0.2 µg/mL, and a trolox equivalent antioxidant capacity of 157.6 and 176.9 µmoles TE per g of peptide determined by two different methods. Analysis by matrix-assisted–laser-desorption-ionization–time-of-flight mass spectrometry (MALDI-TOF MS), followed by the application of bioinformatics tools, enabled the deduction of fourteen theoretical peptide sequences containing antioxidant amino acids at >60%, none of which sequences had been previously reported as antioxidants. Finally, we consider that this 90-min hydrolysate would constitute a promising ingredient in the manufacture of functional foods.
Instituto de Fisiología Vegetal
Centro de Investigación de Proteínas Vegetales
description A partially purified proteolytic extract prepared from Maclura pomifera latex was employed in hydrolyzing a soybean-protein isolate (4.2 mg/mL). The hydrolysis-product formation, monitored by tricine–sodium-dodecyl-sulfate–polyacrylamyde-gel electrophoresis and reverse-phase high-performance liquid chromatography, indicated that after 10 min of reaction the main soybean proteins disappeared. The maximum degree of hydrolysis was 36.2% after a 180-min digestion. The 90-min hydrolysate presented an IC50 of 31.6 ± 0.2 µg/mL, and a trolox equivalent antioxidant capacity of 157.6 and 176.9 µmoles TE per g of peptide determined by two different methods. Analysis by matrix-assisted–laser-desorption-ionization–time-of-flight mass spectrometry (MALDI-TOF MS), followed by the application of bioinformatics tools, enabled the deduction of fourteen theoretical peptide sequences containing antioxidant amino acids at >60%, none of which sequences had been previously reported as antioxidants. Finally, we consider that this 90-min hydrolysate would constitute a promising ingredient in the manufacture of functional foods.
publishDate 2018
dc.date.none.fl_str_mv 2018-05-03
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/10915/127934
url http://sedici.unlp.edu.ar/handle/10915/127934
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1873-7072
info:eu-repo/semantics/altIdentifier/issn/0308-8146
info:eu-repo/semantics/altIdentifier/pmid/29853383
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodchem.2018.05.013
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
326-333
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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