Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide

The aim of this work was to evaluate the effect of the presence of casein glycomacropeptide (CMP) on the in vitro digestibility and potential allergenicity of β-lactoglobulin (β-lg)-CMP mixtures. The digestion products were analyzed by RP-HPLC and RP-HPLC-ESI-MS/MS. The potential allergenicity of th...

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Autores principales:	Martínez, María Julia, Pilosof, Ana María Renata
Publicado:	2016
Materias:	Allergenicity Digestion Interactions Allergens Beam plasma interactions Casein Sludge digestion Allergic symptoms Beta-lactoglobulin Casein glycomacropeptide Digestion products IgE bindings In-vitro digestions Serum samples Mixtures beta lactoglobulin casein casein glycomacropeptide glycoprotein immunoglobulin E unclassified drug allergen caseinomacropeptide epitope lactoglobulin peptide fragment allergenicity Article complex formation differential scanning calorimetry digestion freeze drying high performance liquid chromatography human immunogenicity immunoreactivity in vitro study light scattering nonhuman particle size protein binding protein expression protein function protein protein interaction stomach juice tandem mass spectrometry child electrospray mass spectrometry enzyme linked immunosorbent assay immunology metabolism milk allergy Caseins Child Chromatography, High Pressure Liquid Enzyme-Linked Immunosorbent Assay Epitopes Humans Immunoglobulin E Lactoglobulins Milk Hypersensitivity Peptide Fragments Spectrometry, Mass, Electrospray Ionization Tandem Mass Spectrometry
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03088146_v192_n_p943_Martinez http://hdl.handle.net/20.500.12110/paper_03088146_v192_n_p943_Martinez
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_03088146_v192_n_p943_Martinez
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spelling	paper:paper_03088146_v192_n_p943_Martinez2023-06-08T15:31:43Z Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide Martínez, María Julia Pilosof, Ana María Renata Allergenicity Digestion Interactions Allergens Beam plasma interactions Casein Sludge digestion Allergenicity Allergic symptoms Beta-lactoglobulin Casein glycomacropeptide Digestion products IgE bindings In-vitro digestions Serum samples Mixtures beta lactoglobulin casein casein glycomacropeptide glycoprotein immunoglobulin E unclassified drug allergen casein caseinomacropeptide epitope immunoglobulin E lactoglobulin peptide fragment allergenicity Article complex formation differential scanning calorimetry digestion freeze drying high performance liquid chromatography human immunogenicity immunoreactivity in vitro study light scattering nonhuman particle size protein binding protein expression protein function protein protein interaction stomach juice tandem mass spectrometry child digestion electrospray mass spectrometry enzyme linked immunosorbent assay immunology metabolism milk allergy Allergens Caseins Child Chromatography, High Pressure Liquid Digestion Enzyme-Linked Immunosorbent Assay Epitopes Humans Immunoglobulin E Lactoglobulins Milk Hypersensitivity Peptide Fragments Spectrometry, Mass, Electrospray Ionization Tandem Mass Spectrometry The aim of this work was to evaluate the effect of the presence of casein glycomacropeptide (CMP) on the in vitro digestibility and potential allergenicity of β-lactoglobulin (β-lg)-CMP mixtures. The digestion products were analyzed by RP-HPLC and RP-HPLC-ESI-MS/MS. The potential allergenicity of the digestion products was studied by human IgE binding by inhibition ELISA with serum samples from children with clinical allergic symptoms to β-lg. No differences were observed by HPLC in the mixtures hydrolysates due to CMP-β-lg interactions. RP-HPLC-ESI-MS/MS results showed different peptides occurring in the mixtures hydrolysates. Additionally, it was observed a significant reduction of β-lg IgE binding in the presence of CMP. The disappearance of epitopes in the digested mixtures could explain the lower IgE binding observed in these systems compared to β-lg. It can be concluded that the presence of CMP in products containing β-lg may modify the digestion products that may reduce the potential allergenicity of β-lg. © 2015 Elsevier Ltd. All rights reserved. Fil:Martinez, M.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pilosof, A.M.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2016 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03088146_v192_n_p943_Martinez http://hdl.handle.net/20.500.12110/paper_03088146_v192_n_p943_Martinez
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Allergenicity Digestion Interactions Allergens Beam plasma interactions Casein Sludge digestion Allergenicity Allergic symptoms Beta-lactoglobulin Casein glycomacropeptide Digestion products IgE bindings In-vitro digestions Serum samples Mixtures beta lactoglobulin casein casein glycomacropeptide glycoprotein immunoglobulin E unclassified drug allergen casein caseinomacropeptide epitope immunoglobulin E lactoglobulin peptide fragment allergenicity Article complex formation differential scanning calorimetry digestion freeze drying high performance liquid chromatography human immunogenicity immunoreactivity in vitro study light scattering nonhuman particle size protein binding protein expression protein function protein protein interaction stomach juice tandem mass spectrometry child digestion electrospray mass spectrometry enzyme linked immunosorbent assay immunology metabolism milk allergy Allergens Caseins Child Chromatography, High Pressure Liquid Digestion Enzyme-Linked Immunosorbent Assay Epitopes Humans Immunoglobulin E Lactoglobulins Milk Hypersensitivity Peptide Fragments Spectrometry, Mass, Electrospray Ionization Tandem Mass Spectrometry
spellingShingle	Allergenicity Digestion Interactions Allergens Beam plasma interactions Casein Sludge digestion Allergenicity Allergic symptoms Beta-lactoglobulin Casein glycomacropeptide Digestion products IgE bindings In-vitro digestions Serum samples Mixtures beta lactoglobulin casein casein glycomacropeptide glycoprotein immunoglobulin E unclassified drug allergen casein caseinomacropeptide epitope immunoglobulin E lactoglobulin peptide fragment allergenicity Article complex formation differential scanning calorimetry digestion freeze drying high performance liquid chromatography human immunogenicity immunoreactivity in vitro study light scattering nonhuman particle size protein binding protein expression protein function protein protein interaction stomach juice tandem mass spectrometry child digestion electrospray mass spectrometry enzyme linked immunosorbent assay immunology metabolism milk allergy Allergens Caseins Child Chromatography, High Pressure Liquid Digestion Enzyme-Linked Immunosorbent Assay Epitopes Humans Immunoglobulin E Lactoglobulins Milk Hypersensitivity Peptide Fragments Spectrometry, Mass, Electrospray Ionization Tandem Mass Spectrometry Martínez, María Julia Pilosof, Ana María Renata Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide
topic_facet	Allergenicity Digestion Interactions Allergens Beam plasma interactions Casein Sludge digestion Allergenicity Allergic symptoms Beta-lactoglobulin Casein glycomacropeptide Digestion products IgE bindings In-vitro digestions Serum samples Mixtures beta lactoglobulin casein casein glycomacropeptide glycoprotein immunoglobulin E unclassified drug allergen casein caseinomacropeptide epitope immunoglobulin E lactoglobulin peptide fragment allergenicity Article complex formation differential scanning calorimetry digestion freeze drying high performance liquid chromatography human immunogenicity immunoreactivity in vitro study light scattering nonhuman particle size protein binding protein expression protein function protein protein interaction stomach juice tandem mass spectrometry child digestion electrospray mass spectrometry enzyme linked immunosorbent assay immunology metabolism milk allergy Allergens Caseins Child Chromatography, High Pressure Liquid Digestion Enzyme-Linked Immunosorbent Assay Epitopes Humans Immunoglobulin E Lactoglobulins Milk Hypersensitivity Peptide Fragments Spectrometry, Mass, Electrospray Ionization Tandem Mass Spectrometry
description	The aim of this work was to evaluate the effect of the presence of casein glycomacropeptide (CMP) on the in vitro digestibility and potential allergenicity of β-lactoglobulin (β-lg)-CMP mixtures. The digestion products were analyzed by RP-HPLC and RP-HPLC-ESI-MS/MS. The potential allergenicity of the digestion products was studied by human IgE binding by inhibition ELISA with serum samples from children with clinical allergic symptoms to β-lg. No differences were observed by HPLC in the mixtures hydrolysates due to CMP-β-lg interactions. RP-HPLC-ESI-MS/MS results showed different peptides occurring in the mixtures hydrolysates. Additionally, it was observed a significant reduction of β-lg IgE binding in the presence of CMP. The disappearance of epitopes in the digested mixtures could explain the lower IgE binding observed in these systems compared to β-lg. It can be concluded that the presence of CMP in products containing β-lg may modify the digestion products that may reduce the potential allergenicity of β-lg. © 2015 Elsevier Ltd. All rights reserved.
author	Martínez, María Julia Pilosof, Ana María Renata
author_facet	Martínez, María Julia Pilosof, Ana María Renata
author_sort	Martínez, María Julia
title	Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide
title_short	Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide
title_full	Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide
title_fullStr	Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide
title_full_unstemmed	Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide
title_sort	reduced β-lactoglobulin ige binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide
publishDate	2016
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03088146_v192_n_p943_Martinez http://hdl.handle.net/20.500.12110/paper_03088146_v192_n_p943_Martinez
work_keys_str_mv	AT martinezmariajulia reducedblactoglobulinigebindinguponinvitrodigestionasaresultoftheinteractionoftheproteinwithcaseinglycomacropeptide AT pilosofanamariarenata reducedblactoglobulinigebindinguponinvitrodigestionasaresultoftheinteractionoftheproteinwithcaseinglycomacropeptide
_version_	1768545832774139904

Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide

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