Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer’s spent grain by consecutive chromatography and mass spectrometry

Autores
Garzón, Antonela Guadalupe; Cian, Raúl Esteban; Aquino, Marilín Estefanía; Drago, Silvina Rosa
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The isolation and identification of cholesterol esterase (CE) and pancreatic lipase (PL) inhibitory peptides obtained from the protein hydrolysate of brewer's spent grain (BSG) was performed. BSG peptides were fractionated and purified sequentially by anion exchange, gel filtration (FPLC), and reversed phase high-performance liquid chromatography (RP-HPLC). The fractions obtained from each chromatographic step were collected and the in vitro enzyme inhibitory activity was evaluated. The chromatographic purification process increased the in vitro activities. The most active fractions were evaluated using MALDI-TOF tandem mass spectrometry, which identified three peptides: a peptide with the highest CE inhibition capacity (WNIHMEHQDLTTME) and two peptides with PL inhibition capacity (DFGIASF and LAAVEALSTNG). These three peptides showed hydrophobic and acidic amino acid residues (Asp and Glu) and/or their amines (Asn and Gln), which could be a common feature among lipid-lowering peptides related to CE and PL enzyme inhibition. The in silico studies showed that the three peptides had high hydrophobicity and were susceptible to enzymatic hydrolysis performed by trypsin, pepsin, and pancreatin. The BSG byproduct was a good source of CE and PL inhibitory peptides, thus adding value to this byproduct of the beer industry. This is the first report to demonstrate that BSG peptides can inhibit CE and PL enzymes. This journal is
Fil: Garzón, Antonela Guadalupe. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Cian, Raúl Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Aquino, Marilín Estefanía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Drago, Silvina Rosa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Materia
CHOLESTEROL ESTERASE INHIBITION
PANCREATIC LIPASE INHIBITION
BREWER'S SPENT GRAIN
CHROMATOGRAPHY PROCESS
MALDI-TOF
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:11336/174522

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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer’s spent grain by consecutive chromatography and mass spectrometryGarzón, Antonela GuadalupeCian, Raúl EstebanAquino, Marilín EstefaníaDrago, Silvina RosaCHOLESTEROL ESTERASE INHIBITIONPANCREATIC LIPASE INHIBITIONBREWER'S SPENT GRAINCHROMATOGRAPHY PROCESSMALDI-TOFhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2The isolation and identification of cholesterol esterase (CE) and pancreatic lipase (PL) inhibitory peptides obtained from the protein hydrolysate of brewer's spent grain (BSG) was performed. BSG peptides were fractionated and purified sequentially by anion exchange, gel filtration (FPLC), and reversed phase high-performance liquid chromatography (RP-HPLC). The fractions obtained from each chromatographic step were collected and the in vitro enzyme inhibitory activity was evaluated. The chromatographic purification process increased the in vitro activities. The most active fractions were evaluated using MALDI-TOF tandem mass spectrometry, which identified three peptides: a peptide with the highest CE inhibition capacity (WNIHMEHQDLTTME) and two peptides with PL inhibition capacity (DFGIASF and LAAVEALSTNG). These three peptides showed hydrophobic and acidic amino acid residues (Asp and Glu) and/or their amines (Asn and Gln), which could be a common feature among lipid-lowering peptides related to CE and PL enzyme inhibition. The in silico studies showed that the three peptides had high hydrophobicity and were susceptible to enzymatic hydrolysis performed by trypsin, pepsin, and pancreatin. The BSG byproduct was a good source of CE and PL inhibitory peptides, thus adding value to this byproduct of the beer industry. This is the first report to demonstrate that BSG peptides can inhibit CE and PL enzymes. This journal isFil: Garzón, Antonela Guadalupe. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Cian, Raúl Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Aquino, Marilín Estefanía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Drago, Silvina Rosa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaRoyal Society of Chemistry2020-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/174522Garzón, Antonela Guadalupe; Cian, Raúl Esteban; Aquino, Marilín Estefanía; Drago, Silvina Rosa; Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer’s spent grain by consecutive chromatography and mass spectrometry; Royal Society of Chemistry; Food and Function; 11; 6; 6-2020; 4994-50032042-64962042-650XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2020/FO/D0FO00880Jinfo:eu-repo/semantics/altIdentifier/doi/10.1039/D0FO00880Jinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:00:06Zoai:ri.conicet.gov.ar:11336/174522instacron: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:34982025-09-29 10:00:06.759CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer’s spent grain by consecutive chromatography and mass spectrometry
title Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer’s spent grain by consecutive chromatography and mass spectrometry
spellingShingle Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer’s spent grain by consecutive chromatography and mass spectrometry
Garzón, Antonela Guadalupe
CHOLESTEROL ESTERASE INHIBITION
PANCREATIC LIPASE INHIBITION
BREWER'S SPENT GRAIN
CHROMATOGRAPHY PROCESS
MALDI-TOF
title_short Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer’s spent grain by consecutive chromatography and mass spectrometry
title_full Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer’s spent grain by consecutive chromatography and mass spectrometry
title_fullStr Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer’s spent grain by consecutive chromatography and mass spectrometry
title_full_unstemmed Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer’s spent grain by consecutive chromatography and mass spectrometry
title_sort Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer’s spent grain by consecutive chromatography and mass spectrometry
dc.creator.none.fl_str_mv Garzón, Antonela Guadalupe
Cian, Raúl Esteban
Aquino, Marilín Estefanía
Drago, Silvina Rosa
author Garzón, Antonela Guadalupe
author_facet Garzón, Antonela Guadalupe
Cian, Raúl Esteban
Aquino, Marilín Estefanía
Drago, Silvina Rosa
author_role author
author2 Cian, Raúl Esteban
Aquino, Marilín Estefanía
Drago, Silvina Rosa
author2_role author
author
author
dc.subject.none.fl_str_mv CHOLESTEROL ESTERASE INHIBITION
PANCREATIC LIPASE INHIBITION
BREWER'S SPENT GRAIN
CHROMATOGRAPHY PROCESS
MALDI-TOF
topic CHOLESTEROL ESTERASE INHIBITION
PANCREATIC LIPASE INHIBITION
BREWER'S SPENT GRAIN
CHROMATOGRAPHY PROCESS
MALDI-TOF
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The isolation and identification of cholesterol esterase (CE) and pancreatic lipase (PL) inhibitory peptides obtained from the protein hydrolysate of brewer's spent grain (BSG) was performed. BSG peptides were fractionated and purified sequentially by anion exchange, gel filtration (FPLC), and reversed phase high-performance liquid chromatography (RP-HPLC). The fractions obtained from each chromatographic step were collected and the in vitro enzyme inhibitory activity was evaluated. The chromatographic purification process increased the in vitro activities. The most active fractions were evaluated using MALDI-TOF tandem mass spectrometry, which identified three peptides: a peptide with the highest CE inhibition capacity (WNIHMEHQDLTTME) and two peptides with PL inhibition capacity (DFGIASF and LAAVEALSTNG). These three peptides showed hydrophobic and acidic amino acid residues (Asp and Glu) and/or their amines (Asn and Gln), which could be a common feature among lipid-lowering peptides related to CE and PL enzyme inhibition. The in silico studies showed that the three peptides had high hydrophobicity and were susceptible to enzymatic hydrolysis performed by trypsin, pepsin, and pancreatin. The BSG byproduct was a good source of CE and PL inhibitory peptides, thus adding value to this byproduct of the beer industry. This is the first report to demonstrate that BSG peptides can inhibit CE and PL enzymes. This journal is
Fil: Garzón, Antonela Guadalupe. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Cian, Raúl Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Aquino, Marilín Estefanía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Drago, Silvina Rosa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
description The isolation and identification of cholesterol esterase (CE) and pancreatic lipase (PL) inhibitory peptides obtained from the protein hydrolysate of brewer's spent grain (BSG) was performed. BSG peptides were fractionated and purified sequentially by anion exchange, gel filtration (FPLC), and reversed phase high-performance liquid chromatography (RP-HPLC). The fractions obtained from each chromatographic step were collected and the in vitro enzyme inhibitory activity was evaluated. The chromatographic purification process increased the in vitro activities. The most active fractions were evaluated using MALDI-TOF tandem mass spectrometry, which identified three peptides: a peptide with the highest CE inhibition capacity (WNIHMEHQDLTTME) and two peptides with PL inhibition capacity (DFGIASF and LAAVEALSTNG). These three peptides showed hydrophobic and acidic amino acid residues (Asp and Glu) and/or their amines (Asn and Gln), which could be a common feature among lipid-lowering peptides related to CE and PL enzyme inhibition. The in silico studies showed that the three peptides had high hydrophobicity and were susceptible to enzymatic hydrolysis performed by trypsin, pepsin, and pancreatin. The BSG byproduct was a good source of CE and PL inhibitory peptides, thus adding value to this byproduct of the beer industry. This is the first report to demonstrate that BSG peptides can inhibit CE and PL enzymes. This journal is
publishDate 2020
dc.date.none.fl_str_mv 2020-06
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/11336/174522
Garzón, Antonela Guadalupe; Cian, Raúl Esteban; Aquino, Marilín Estefanía; Drago, Silvina Rosa; Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer’s spent grain by consecutive chromatography and mass spectrometry; Royal Society of Chemistry; Food and Function; 11; 6; 6-2020; 4994-5003
2042-6496
2042-650X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/174522
identifier_str_mv Garzón, Antonela Guadalupe; Cian, Raúl Esteban; Aquino, Marilín Estefanía; Drago, Silvina Rosa; Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer’s spent grain by consecutive chromatography and mass spectrometry; Royal Society of Chemistry; Food and Function; 11; 6; 6-2020; 4994-5003
2042-6496
2042-650X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2020/FO/D0FO00880J
info:eu-repo/semantics/altIdentifier/doi/10.1039/D0FO00880J
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
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Royal Society of Chemistry
publisher.none.fl_str_mv Royal Society of Chemistry
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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