Anti-diabetic properties of brewer's spent yeast peptides: In vitro, in silico and ex vivo study after simulated gastrointestinal digestion

Autores
Aquino, Marilín Estefanía; Drago, Silvina Rosa; Sánchez de Medina, Fermín; Martínez Augustin, Olga; Cian, Raúl Esteban
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Brewer´s spent yeast (BSY) hydrolysates are a source of antidiabetic peptides. Nevertheless, the impact of in vitro gastrointestinal digestion of BSY derived peptides on diabetes has not been assessed. In this study, two BSY hydrolysates were obtained (H1 and H2) using β-glucanase and alkaline protease, with either 1 h or 2 h hydrolysis time for H1 and H2, respectively. These hydrolysates were then subjected to simulated gastrointestinal digestion (SGID), obtaining dialysates D1 and D2, respectively. BSY hydrolysates inhibited the activity of α-glucosidase and dipeptidyl peptidase IV (DPP-IV) enzymes. Moreover, although D2 was inactive against these enzymes, D1 IC50 value was lower than those found for the hydrolysates. Interestingly, after electrophoretic separation, D1 mannose-linked peptides showed the highest α-glucosidase inhibitory activity, while non-glycosylated peptides had the highest DPP-IV inhibitory activity. Kinetic analyses showed a non-competitive mechanism in both cases. After peptide identification, GILFVGSGVSGGEEGAR and IINEPTAAAIAYGLDK showed the highest in silico anti-diabetic activities among mannose-linked and non-glycosylated peptides, respectively (AntiDMPpred score: 0.70 and 0.77). Molecular docking also indicated that these peptides act as non-competitive inhibitors. Finally, an ex vivo model of mouse jejunum organoids was used to study the effect of D1 on the expression of intestinal epithelial genes related to diabetes. The reduction of the expression of genes that codify lactase, sucrase-isomaltase and glucose transporter 2 was observed, as well as an increase in the expression of Gip (glucose-dependent insulinotropic peptide) and Glp1 (glucagon-like peptide 1). This is the first report to evaluate the anti-diabetic effect of BSY peptides in mouse jejunum organoids.
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
Fil: Sánchez de Medina, Fermín. Universidad de Granada. Facultad de Farmacia.; España
Fil: Martínez Augustin, Olga. Universidad de Granada. Facultad de Farmacia.; España
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
Materia
ANTI-DIABETIC PROPERTIES
BREWER'S SPENT YEAST PEPTIDES
SIMULATED GASTROINTESTINAL DIGESTION
MOUSE JEJUNUM ORGANOIDS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/233450
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/233450
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Anti-diabetic properties of brewer's spent yeast peptides: In vitro, in silico and ex vivo study after simulated gastrointestinal digestionAquino, Marilín EstefaníaDrago, Silvina RosaSánchez de Medina, FermínMartínez Augustin, OlgaCian, Raúl EstebanANTI-DIABETIC PROPERTIESBREWER'S SPENT YEAST PEPTIDESSIMULATED GASTROINTESTINAL DIGESTIONMOUSE JEJUNUM ORGANOIDShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Brewer´s spent yeast (BSY) hydrolysates are a source of antidiabetic peptides. Nevertheless, the impact of in vitro gastrointestinal digestion of BSY derived peptides on diabetes has not been assessed. In this study, two BSY hydrolysates were obtained (H1 and H2) using β-glucanase and alkaline protease, with either 1 h or 2 h hydrolysis time for H1 and H2, respectively. These hydrolysates were then subjected to simulated gastrointestinal digestion (SGID), obtaining dialysates D1 and D2, respectively. BSY hydrolysates inhibited the activity of α-glucosidase and dipeptidyl peptidase IV (DPP-IV) enzymes. Moreover, although D2 was inactive against these enzymes, D1 IC50 value was lower than those found for the hydrolysates. Interestingly, after electrophoretic separation, D1 mannose-linked peptides showed the highest α-glucosidase inhibitory activity, while non-glycosylated peptides had the highest DPP-IV inhibitory activity. Kinetic analyses showed a non-competitive mechanism in both cases. After peptide identification, GILFVGSGVSGGEEGAR and IINEPTAAAIAYGLDK showed the highest in silico anti-diabetic activities among mannose-linked and non-glycosylated peptides, respectively (AntiDMPpred score: 0.70 and 0.77). Molecular docking also indicated that these peptides act as non-competitive inhibitors. Finally, an ex vivo model of mouse jejunum organoids was used to study the effect of D1 on the expression of intestinal epithelial genes related to diabetes. The reduction of the expression of genes that codify lactase, sucrase-isomaltase and glucose transporter 2 was observed, as well as an increase in the expression of Gip (glucose-dependent insulinotropic peptide) and Glp1 (glucagon-like peptide 1). This is the first report to evaluate the anti-diabetic effect of BSY peptides in mouse jejunum organoids.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; 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; ArgentinaFil: Sánchez de Medina, Fermín. Universidad de Granada. Facultad de Farmacia.; EspañaFil: Martínez Augustin, Olga. Universidad de Granada. Facultad de Farmacia.; EspañaFil: 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; ArgentinaRoyal Society of Chemistry2024-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/233450Aquino, Marilín Estefanía; Drago, Silvina Rosa; Sánchez de Medina, Fermín; Martínez Augustin, Olga; Cian, Raúl Esteban; Anti-diabetic properties of brewer's spent yeast peptides: In vitro, in silico and ex vivo study after simulated gastrointestinal digestion; Royal Society of Chemistry; Food & Function; 15; 7; 3-2024; 3778-37902042-64962042-650XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/content/articlelanding/2024/fo/d3fo04040binfo:eu-repo/semantics/altIdentifier/doi/10.1039/D3FO04040Binfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:03:33Zoai:ri.conicet.gov.ar:11336/233450instacron: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 10:03:33.449CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Anti-diabetic properties of brewer's spent yeast peptides: In vitro, in silico and ex vivo study after simulated gastrointestinal digestion
title Anti-diabetic properties of brewer's spent yeast peptides: In vitro, in silico and ex vivo study after simulated gastrointestinal digestion
spellingShingle Anti-diabetic properties of brewer's spent yeast peptides: In vitro, in silico and ex vivo study after simulated gastrointestinal digestion
Aquino, Marilín Estefanía
ANTI-DIABETIC PROPERTIES
BREWER'S SPENT YEAST PEPTIDES
SIMULATED GASTROINTESTINAL DIGESTION
MOUSE JEJUNUM ORGANOIDS
title_short Anti-diabetic properties of brewer's spent yeast peptides: In vitro, in silico and ex vivo study after simulated gastrointestinal digestion
title_full Anti-diabetic properties of brewer's spent yeast peptides: In vitro, in silico and ex vivo study after simulated gastrointestinal digestion
title_fullStr Anti-diabetic properties of brewer's spent yeast peptides: In vitro, in silico and ex vivo study after simulated gastrointestinal digestion
title_full_unstemmed Anti-diabetic properties of brewer's spent yeast peptides: In vitro, in silico and ex vivo study after simulated gastrointestinal digestion
title_sort Anti-diabetic properties of brewer's spent yeast peptides: In vitro, in silico and ex vivo study after simulated gastrointestinal digestion
dc.creator.none.fl_str_mv Aquino, Marilín Estefanía
Drago, Silvina Rosa
Sánchez de Medina, Fermín
Martínez Augustin, Olga
Cian, Raúl Esteban
author Aquino, Marilín Estefanía
author_facet Aquino, Marilín Estefanía
Drago, Silvina Rosa
Sánchez de Medina, Fermín
Martínez Augustin, Olga
Cian, Raúl Esteban
author_role author
author2 Drago, Silvina Rosa
Sánchez de Medina, Fermín
Martínez Augustin, Olga
Cian, Raúl Esteban
author2_role author
author
author
author
dc.subject.none.fl_str_mv ANTI-DIABETIC PROPERTIES
BREWER'S SPENT YEAST PEPTIDES
SIMULATED GASTROINTESTINAL DIGESTION
MOUSE JEJUNUM ORGANOIDS
topic ANTI-DIABETIC PROPERTIES
BREWER'S SPENT YEAST PEPTIDES
SIMULATED GASTROINTESTINAL DIGESTION
MOUSE JEJUNUM ORGANOIDS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Brewer´s spent yeast (BSY) hydrolysates are a source of antidiabetic peptides. Nevertheless, the impact of in vitro gastrointestinal digestion of BSY derived peptides on diabetes has not been assessed. In this study, two BSY hydrolysates were obtained (H1 and H2) using β-glucanase and alkaline protease, with either 1 h or 2 h hydrolysis time for H1 and H2, respectively. These hydrolysates were then subjected to simulated gastrointestinal digestion (SGID), obtaining dialysates D1 and D2, respectively. BSY hydrolysates inhibited the activity of α-glucosidase and dipeptidyl peptidase IV (DPP-IV) enzymes. Moreover, although D2 was inactive against these enzymes, D1 IC50 value was lower than those found for the hydrolysates. Interestingly, after electrophoretic separation, D1 mannose-linked peptides showed the highest α-glucosidase inhibitory activity, while non-glycosylated peptides had the highest DPP-IV inhibitory activity. Kinetic analyses showed a non-competitive mechanism in both cases. After peptide identification, GILFVGSGVSGGEEGAR and IINEPTAAAIAYGLDK showed the highest in silico anti-diabetic activities among mannose-linked and non-glycosylated peptides, respectively (AntiDMPpred score: 0.70 and 0.77). Molecular docking also indicated that these peptides act as non-competitive inhibitors. Finally, an ex vivo model of mouse jejunum organoids was used to study the effect of D1 on the expression of intestinal epithelial genes related to diabetes. The reduction of the expression of genes that codify lactase, sucrase-isomaltase and glucose transporter 2 was observed, as well as an increase in the expression of Gip (glucose-dependent insulinotropic peptide) and Glp1 (glucagon-like peptide 1). This is the first report to evaluate the anti-diabetic effect of BSY peptides in mouse jejunum organoids.
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
Fil: Sánchez de Medina, Fermín. Universidad de Granada. Facultad de Farmacia.; España
Fil: Martínez Augustin, Olga. Universidad de Granada. Facultad de Farmacia.; España
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
description Brewer´s spent yeast (BSY) hydrolysates are a source of antidiabetic peptides. Nevertheless, the impact of in vitro gastrointestinal digestion of BSY derived peptides on diabetes has not been assessed. In this study, two BSY hydrolysates were obtained (H1 and H2) using β-glucanase and alkaline protease, with either 1 h or 2 h hydrolysis time for H1 and H2, respectively. These hydrolysates were then subjected to simulated gastrointestinal digestion (SGID), obtaining dialysates D1 and D2, respectively. BSY hydrolysates inhibited the activity of α-glucosidase and dipeptidyl peptidase IV (DPP-IV) enzymes. Moreover, although D2 was inactive against these enzymes, D1 IC50 value was lower than those found for the hydrolysates. Interestingly, after electrophoretic separation, D1 mannose-linked peptides showed the highest α-glucosidase inhibitory activity, while non-glycosylated peptides had the highest DPP-IV inhibitory activity. Kinetic analyses showed a non-competitive mechanism in both cases. After peptide identification, GILFVGSGVSGGEEGAR and IINEPTAAAIAYGLDK showed the highest in silico anti-diabetic activities among mannose-linked and non-glycosylated peptides, respectively (AntiDMPpred score: 0.70 and 0.77). Molecular docking also indicated that these peptides act as non-competitive inhibitors. Finally, an ex vivo model of mouse jejunum organoids was used to study the effect of D1 on the expression of intestinal epithelial genes related to diabetes. The reduction of the expression of genes that codify lactase, sucrase-isomaltase and glucose transporter 2 was observed, as well as an increase in the expression of Gip (glucose-dependent insulinotropic peptide) and Glp1 (glucagon-like peptide 1). This is the first report to evaluate the anti-diabetic effect of BSY peptides in mouse jejunum organoids.
publishDate 2024
dc.date.none.fl_str_mv 2024-03
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/11336/233450
Aquino, Marilín Estefanía; Drago, Silvina Rosa; Sánchez de Medina, Fermín; Martínez Augustin, Olga; Cian, Raúl Esteban; Anti-diabetic properties of brewer's spent yeast peptides: In vitro, in silico and ex vivo study after simulated gastrointestinal digestion; Royal Society of Chemistry; Food & Function; 15; 7; 3-2024; 3778-3790
2042-6496
2042-650X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/233450
identifier_str_mv Aquino, Marilín Estefanía; Drago, Silvina Rosa; Sánchez de Medina, Fermín; Martínez Augustin, Olga; Cian, Raúl Esteban; Anti-diabetic properties of brewer's spent yeast peptides: In vitro, in silico and ex vivo study after simulated gastrointestinal digestion; Royal Society of Chemistry; Food & Function; 15; 7; 3-2024; 3778-3790
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/https://pubs.rsc.org/en/content/articlelanding/2024/fo/d3fo04040b
info:eu-repo/semantics/altIdentifier/doi/10.1039/D3FO04040B
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.format.none.fl_str_mv application/pdf
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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score 13.13397

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