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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/174522
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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 |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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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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1844613779129630720 |
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13.070432 |