Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powder

This study aims to evaluate the impact of heat treatment on the hydrolysis kinetics of cow milk proteins and on the peptide release during in vitro dynamic gastric digestion. SDS-PAGE and ELISA techniques were employed to assess the hydrolysis of proteins over time of digestion. The evolution of the...

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Detalles Bibliográficos
Autores: Sánchez-Rivera, Laura, Ménard, Olivia, Recio, Isidra, Dupont, Didier
Tipo de recurso: artículo
Estado:Versión enviada para evaluación y publicación
Fecha de publicación:2015
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/149914
Acceso en línea:http://hdl.handle.net/10261/149914
Access Level:acceso abierto
Palabra clave:Mass spectrometry
Dynamic digestion
Peptidomics
Heat treatment
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spelling Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powderSánchez-Rivera, LauraMénard, OliviaRecio, IsidraDupont, DidierMass spectrometryDynamic digestionPeptidomicsHeat treatmentThis study aims to evaluate the impact of heat treatment on the hydrolysis kinetics of cow milk proteins and on the peptide release during in vitro dynamic gastric digestion. SDS-PAGE and ELISA techniques were employed to assess the hydrolysis of proteins over time of digestion. The evolution of the peptidome generated through dynamic digestion of heated and non-heated milk was studied at different times, using MS-based techniques (ion trap and MALDI-TOF/TOF) coupled to liquid chromatography. The peptide homology value between both samples at the end of digestion (48%) confirmed the impact of heat treatment on the identity of peptides generated during digestion, despite their identical initial protein content and being the same matrix in both cases. Heat treatment produced an increased resistance to hydrolysis by pepsin in the casein fraction. However, β-lactoglobulin was found to be more susceptible to hydrolysis. Although differences on the pattern of peptide release were found between both samples, also some common traits after digestion were observed. The regions comprised between the residues 76-93 of β-casein, where several binding epitopes are included, as well as the β-casein domains 126-140 and 190-209 were found to be resistant to pepsin.This work was partly supported by project AGL2011-24643 from Ministerio de Economía y Competitividad. The authors are participants in the FA1005COST Action INFOGEST on food digestion. L. Sanchez-Rivera wants to acknowledge CSIC for a JAE Program fellowship.Peer ReviewedElsevierMinisterio de Economía y Competitividad (España)European CommissionConsejo Superior de Investigaciones Científicas (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2017201720152017info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Preprintinfo:eu-repo/semantics/submittedVersionhttp://hdl.handle.net/10261/149914reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttps://doi.org/10.1016/j.foodres.2015.08.001Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1499142026-05-22T06:33:51Z
dc.title.none.fl_str_mv Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powder
title Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powder
spellingShingle Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powder
Sánchez-Rivera, Laura
Mass spectrometry
Dynamic digestion
Peptidomics
Heat treatment
title_short Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powder
title_full Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powder
title_fullStr Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powder
title_full_unstemmed Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powder
title_sort Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powder
dc.creator.none.fl_str_mv Sánchez-Rivera, Laura
Ménard, Olivia
Recio, Isidra
Dupont, Didier
author Sánchez-Rivera, Laura
author_facet Sánchez-Rivera, Laura
Ménard, Olivia
Recio, Isidra
Dupont, Didier
author_role author
author2 Ménard, Olivia
Recio, Isidra
Dupont, Didier
author2_role author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía y Competitividad (España)
European Commission
Consejo Superior de Investigaciones Científicas (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Mass spectrometry
Dynamic digestion
Peptidomics
Heat treatment
topic Mass spectrometry
Dynamic digestion
Peptidomics
Heat treatment
description This study aims to evaluate the impact of heat treatment on the hydrolysis kinetics of cow milk proteins and on the peptide release during in vitro dynamic gastric digestion. SDS-PAGE and ELISA techniques were employed to assess the hydrolysis of proteins over time of digestion. The evolution of the peptidome generated through dynamic digestion of heated and non-heated milk was studied at different times, using MS-based techniques (ion trap and MALDI-TOF/TOF) coupled to liquid chromatography. The peptide homology value between both samples at the end of digestion (48%) confirmed the impact of heat treatment on the identity of peptides generated during digestion, despite their identical initial protein content and being the same matrix in both cases. Heat treatment produced an increased resistance to hydrolysis by pepsin in the casein fraction. However, β-lactoglobulin was found to be more susceptible to hydrolysis. Although differences on the pattern of peptide release were found between both samples, also some common traits after digestion were observed. The regions comprised between the residues 76-93 of β-casein, where several binding epitopes are included, as well as the β-casein domains 126-140 and 190-209 were found to be resistant to pepsin.
publishDate 2015
dc.date.none.fl_str_mv 2015
2017
2017
2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Preprint
info:eu-repo/semantics/submittedVersion
format article
status_str submittedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/149914
url http://hdl.handle.net/10261/149914
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://doi.org/10.1016/j.foodres.2015.08.001
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,812429

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