Antioxidant peptides released from soybean by lactic acid bacteria with proteolytic activity

Autores
Quiroga, Maria; Babot, Jaime Daniel; Bertani, Milena Sabrina; Argañaraz Martínez, Fernando Eloy; Perez Chaia, Adriana Beatriz
Año de publicación
2021
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Biopeptides are fragments encrypted in a precursor protein. They possess a particular amino acid sequence and specific biofunctional attributes that can influence the main systems of an organism when released by proteolysis. Glycinin and βconglycinin are the main proteins in soybean (which in turn is the main protein source in poultry feeds), and many amino acidic sequences with different features, such as antioxidant properties, are included in them. On the other hand, microorganisms are an important source of proteolytic enzymes. They could act on soybean proteins and release biofunctional peptides that may possess antioxidant properties. Therefore, the aim of this work was the study of the antioxidant activity of the biopeptides released from soybean protein isolate (SPI, which contains only glycinin and β-conglycinin) by three lactic acid bacteria (Enterococcus italicus LET 302, E. faecium LET 303 and Lactobacillus brevis LET 216) previously isolated from soybean flour. To this end, each strain was incubated for 16 h in broth with SPI as the sole protein source. Then, the supernatants were recovered by centrifugation and sterilized by filtration with 0.22 µm pore membranes. In order to obtain different peptidic fractions, the supernatants were centrifuged with 10 kDa filters, and the filtrates were centrifuged again with 3 kDa filters. This way, three fractions were obtained for each strain: M1 (peptides > 10 kDa), M2 (3 kDa < peptides < 10 kDa), and M3 (peptides < 3 kDa). Protein concentration was assessed by Bradford, and the amount of protein on each fraction was adjusted to 0.3 µg before the antioxidant activity was determined by DPPH assay. Antioxidant activity was observed on the three fractions from all strains, and M3 presented the highest activity in all cases. Comparing the respective fractions from different strains, higher antioxidant activity was always showed by E. faecium LET 303, followed by E. italicus LET 302 and L. brevis LET 216. In conclusion, the proteolytic enzymes expressed by the strains of lactic acid bacteria studied could act on soybean proteins, releasing peptides with antioxidant activity. The hydrolysis of these proteins, in a treatment before their consumption by poultry or in situ by these bacteria administered as feed additive, could improve their digestion as well as collaborate with the oxidative metabolism of cells in the digestive system.
Fil: Quiroga, Maria. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Microbiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Babot, Jaime Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Bertani, Milena Sabrina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Argañaraz Martínez, Fernando Eloy. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Microbiología; Argentina
Fil: Perez Chaia, Adriana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
LVI Annual Meeting Argentine Society for Biochemistry and Molecular Biology; XV Annual Meeting Argentinean Society for General Microbiology
Argentina
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Sociedad Argentina de Microbiología General
Materia
ANTIOXIDANT PEPTIDES
SOYBEAN PROTEIN
LACTIC ACID BACTERIA
PROTEOLYTIC ACTIVITY
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:11336/158446
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Antioxidant peptides released from soybean by lactic acid bacteria with proteolytic activityQuiroga, MariaBabot, Jaime DanielBertani, Milena SabrinaArgañaraz Martínez, Fernando EloyPerez Chaia, Adriana BeatrizANTIOXIDANT PEPTIDESSOYBEAN PROTEINLACTIC ACID BACTERIAPROTEOLYTIC ACTIVITYhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Biopeptides are fragments encrypted in a precursor protein. They possess a particular amino acid sequence and specific biofunctional attributes that can influence the main systems of an organism when released by proteolysis. Glycinin and βconglycinin are the main proteins in soybean (which in turn is the main protein source in poultry feeds), and many amino acidic sequences with different features, such as antioxidant properties, are included in them. On the other hand, microorganisms are an important source of proteolytic enzymes. They could act on soybean proteins and release biofunctional peptides that may possess antioxidant properties. Therefore, the aim of this work was the study of the antioxidant activity of the biopeptides released from soybean protein isolate (SPI, which contains only glycinin and β-conglycinin) by three lactic acid bacteria (Enterococcus italicus LET 302, E. faecium LET 303 and Lactobacillus brevis LET 216) previously isolated from soybean flour. To this end, each strain was incubated for 16 h in broth with SPI as the sole protein source. Then, the supernatants were recovered by centrifugation and sterilized by filtration with 0.22 µm pore membranes. In order to obtain different peptidic fractions, the supernatants were centrifuged with 10 kDa filters, and the filtrates were centrifuged again with 3 kDa filters. This way, three fractions were obtained for each strain: M1 (peptides > 10 kDa), M2 (3 kDa < peptides < 10 kDa), and M3 (peptides < 3 kDa). Protein concentration was assessed by Bradford, and the amount of protein on each fraction was adjusted to 0.3 µg before the antioxidant activity was determined by DPPH assay. Antioxidant activity was observed on the three fractions from all strains, and M3 presented the highest activity in all cases. Comparing the respective fractions from different strains, higher antioxidant activity was always showed by E. faecium LET 303, followed by E. italicus LET 302 and L. brevis LET 216. In conclusion, the proteolytic enzymes expressed by the strains of lactic acid bacteria studied could act on soybean proteins, releasing peptides with antioxidant activity. The hydrolysis of these proteins, in a treatment before their consumption by poultry or in situ by these bacteria administered as feed additive, could improve their digestion as well as collaborate with the oxidative metabolism of cells in the digestive system.Fil: Quiroga, Maria. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Microbiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Babot, Jaime Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Bertani, Milena Sabrina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Argañaraz Martínez, Fernando Eloy. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Microbiología; ArgentinaFil: Perez Chaia, Adriana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaLVI Annual Meeting Argentine Society for Biochemistry and Molecular Biology; XV Annual Meeting Argentinean Society for General MicrobiologyArgentinaSociedad Argentina de Investigación en Bioquímica y Biología MolecularSociedad Argentina de Microbiología GeneralTech Science Press2021info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónJournalhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/158446Antioxidant peptides released from soybean by lactic acid bacteria with proteolytic activity; LVI Annual Meeting Argentine Society for Biochemistry and Molecular Biology; XV Annual Meeting Argentinean Society for General Microbiology; Argentina; 2020; 59-590327-95451667-5746CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.saib.org.ar/congreso/info:eu-repo/semantics/altIdentifier/url/http://www.saib.org.ar/sites/default/files/BIOCELL-SAIB-2020-version-final.pdfNacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:55:07Zoai:ri.conicet.gov.ar:11336/158446instacron: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 09:55:07.917CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Antioxidant peptides released from soybean by lactic acid bacteria with proteolytic activity
title Antioxidant peptides released from soybean by lactic acid bacteria with proteolytic activity
spellingShingle Antioxidant peptides released from soybean by lactic acid bacteria with proteolytic activity
Quiroga, Maria
ANTIOXIDANT PEPTIDES
SOYBEAN PROTEIN
LACTIC ACID BACTERIA
PROTEOLYTIC ACTIVITY
title_short Antioxidant peptides released from soybean by lactic acid bacteria with proteolytic activity
title_full Antioxidant peptides released from soybean by lactic acid bacteria with proteolytic activity
title_fullStr Antioxidant peptides released from soybean by lactic acid bacteria with proteolytic activity
title_full_unstemmed Antioxidant peptides released from soybean by lactic acid bacteria with proteolytic activity
title_sort Antioxidant peptides released from soybean by lactic acid bacteria with proteolytic activity
dc.creator.none.fl_str_mv Quiroga, Maria
Babot, Jaime Daniel
Bertani, Milena Sabrina
Argañaraz Martínez, Fernando Eloy
Perez Chaia, Adriana Beatriz
author Quiroga, Maria
author_facet Quiroga, Maria
Babot, Jaime Daniel
Bertani, Milena Sabrina
Argañaraz Martínez, Fernando Eloy
Perez Chaia, Adriana Beatriz
author_role author
author2 Babot, Jaime Daniel
Bertani, Milena Sabrina
Argañaraz Martínez, Fernando Eloy
Perez Chaia, Adriana Beatriz
author2_role author
author
author
author
dc.subject.none.fl_str_mv ANTIOXIDANT PEPTIDES
SOYBEAN PROTEIN
LACTIC ACID BACTERIA
PROTEOLYTIC ACTIVITY
topic ANTIOXIDANT PEPTIDES
SOYBEAN PROTEIN
LACTIC ACID BACTERIA
PROTEOLYTIC ACTIVITY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Biopeptides are fragments encrypted in a precursor protein. They possess a particular amino acid sequence and specific biofunctional attributes that can influence the main systems of an organism when released by proteolysis. Glycinin and βconglycinin are the main proteins in soybean (which in turn is the main protein source in poultry feeds), and many amino acidic sequences with different features, such as antioxidant properties, are included in them. On the other hand, microorganisms are an important source of proteolytic enzymes. They could act on soybean proteins and release biofunctional peptides that may possess antioxidant properties. Therefore, the aim of this work was the study of the antioxidant activity of the biopeptides released from soybean protein isolate (SPI, which contains only glycinin and β-conglycinin) by three lactic acid bacteria (Enterococcus italicus LET 302, E. faecium LET 303 and Lactobacillus brevis LET 216) previously isolated from soybean flour. To this end, each strain was incubated for 16 h in broth with SPI as the sole protein source. Then, the supernatants were recovered by centrifugation and sterilized by filtration with 0.22 µm pore membranes. In order to obtain different peptidic fractions, the supernatants were centrifuged with 10 kDa filters, and the filtrates were centrifuged again with 3 kDa filters. This way, three fractions were obtained for each strain: M1 (peptides > 10 kDa), M2 (3 kDa < peptides < 10 kDa), and M3 (peptides < 3 kDa). Protein concentration was assessed by Bradford, and the amount of protein on each fraction was adjusted to 0.3 µg before the antioxidant activity was determined by DPPH assay. Antioxidant activity was observed on the three fractions from all strains, and M3 presented the highest activity in all cases. Comparing the respective fractions from different strains, higher antioxidant activity was always showed by E. faecium LET 303, followed by E. italicus LET 302 and L. brevis LET 216. In conclusion, the proteolytic enzymes expressed by the strains of lactic acid bacteria studied could act on soybean proteins, releasing peptides with antioxidant activity. The hydrolysis of these proteins, in a treatment before their consumption by poultry or in situ by these bacteria administered as feed additive, could improve their digestion as well as collaborate with the oxidative metabolism of cells in the digestive system.
Fil: Quiroga, Maria. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Microbiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Babot, Jaime Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Bertani, Milena Sabrina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Argañaraz Martínez, Fernando Eloy. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Microbiología; Argentina
Fil: Perez Chaia, Adriana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
LVI Annual Meeting Argentine Society for Biochemistry and Molecular Biology; XV Annual Meeting Argentinean Society for General Microbiology
Argentina
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Sociedad Argentina de Microbiología General
description Biopeptides are fragments encrypted in a precursor protein. They possess a particular amino acid sequence and specific biofunctional attributes that can influence the main systems of an organism when released by proteolysis. Glycinin and βconglycinin are the main proteins in soybean (which in turn is the main protein source in poultry feeds), and many amino acidic sequences with different features, such as antioxidant properties, are included in them. On the other hand, microorganisms are an important source of proteolytic enzymes. They could act on soybean proteins and release biofunctional peptides that may possess antioxidant properties. Therefore, the aim of this work was the study of the antioxidant activity of the biopeptides released from soybean protein isolate (SPI, which contains only glycinin and β-conglycinin) by three lactic acid bacteria (Enterococcus italicus LET 302, E. faecium LET 303 and Lactobacillus brevis LET 216) previously isolated from soybean flour. To this end, each strain was incubated for 16 h in broth with SPI as the sole protein source. Then, the supernatants were recovered by centrifugation and sterilized by filtration with 0.22 µm pore membranes. In order to obtain different peptidic fractions, the supernatants were centrifuged with 10 kDa filters, and the filtrates were centrifuged again with 3 kDa filters. This way, three fractions were obtained for each strain: M1 (peptides > 10 kDa), M2 (3 kDa < peptides < 10 kDa), and M3 (peptides < 3 kDa). Protein concentration was assessed by Bradford, and the amount of protein on each fraction was adjusted to 0.3 µg before the antioxidant activity was determined by DPPH assay. Antioxidant activity was observed on the three fractions from all strains, and M3 presented the highest activity in all cases. Comparing the respective fractions from different strains, higher antioxidant activity was always showed by E. faecium LET 303, followed by E. italicus LET 302 and L. brevis LET 216. In conclusion, the proteolytic enzymes expressed by the strains of lactic acid bacteria studied could act on soybean proteins, releasing peptides with antioxidant activity. The hydrolysis of these proteins, in a treatment before their consumption by poultry or in situ by these bacteria administered as feed additive, could improve their digestion as well as collaborate with the oxidative metabolism of cells in the digestive system.
publishDate 2021
dc.date.none.fl_str_mv 2021
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Reunión
Journal
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/158446
Antioxidant peptides released from soybean by lactic acid bacteria with proteolytic activity; LVI Annual Meeting Argentine Society for Biochemistry and Molecular Biology; XV Annual Meeting Argentinean Society for General Microbiology; Argentina; 2020; 59-59
0327-9545
1667-5746
CONICET Digital
CONICET
url http://hdl.handle.net/11336/158446
identifier_str_mv Antioxidant peptides released from soybean by lactic acid bacteria with proteolytic activity; LVI Annual Meeting Argentine Society for Biochemistry and Molecular Biology; XV Annual Meeting Argentinean Society for General Microbiology; Argentina; 2020; 59-59
0327-9545
1667-5746
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/url/http://www.saib.org.ar/sites/default/files/BIOCELL-SAIB-2020-version-final.pdf
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
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application/pdf
application/pdf
dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Tech Science Press
publisher.none.fl_str_mv Tech Science Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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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
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