Maillard induced glycation behaviour of individual milk proteins

This paper set out to differentiate the Maillard induced glycation reactivity of individual milk proteins using different saccharides under well-defined reaction conditions. α-Lactalbumin, β-lactoglobulin and β-casein were incubated with mono-, di- and trisaccharides in the dry state under standardised buffered conditions and glycation was expressed relative to the available reactive groups per protein (DG). Protein reactivity, described by the DG max and initial speed of glycation (v), followed the same order for each protein-saccharide incubation: α-lactalbumin > β-lactoglobulin ≫ β-casein. Glycation of whey proteins by different monosaccharides was double that of β-casein. Differences in DG between whey proteins and β-casein decreased with increased saccharide size. A two-fold difference was found for glycation in the presence of the dimers lactose and maltose for β-casein but not for the whey proteins. The percentage of glycated lysines increased with increased lysine to protein size ratio.

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Bibliographic Details
Main Authors: Cardoso, Hugo B., Wierenga, Peter A., Gruppen, Harry, Schols, Henk A.
Format: Article/Letter to editor biblioteca
Language:English
Subjects:Reactivity, α-Lactalbumin, β-Casein, β-Lactoglobulin,
Online Access:https://research.wur.nl/en/publications/maillard-induced-glycation-behaviour-of-individual-milk-proteins
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spelling dig-wur-nl-wurpubs-5339012024-10-02 Cardoso, Hugo B. Wierenga, Peter A. Gruppen, Harry Schols, Henk A. Article/Letter to editor Food Chemistry 252 (2018) ISSN: 0308-8146 Maillard induced glycation behaviour of individual milk proteins 2018 This paper set out to differentiate the Maillard induced glycation reactivity of individual milk proteins using different saccharides under well-defined reaction conditions. α-Lactalbumin, β-lactoglobulin and β-casein were incubated with mono-, di- and trisaccharides in the dry state under standardised buffered conditions and glycation was expressed relative to the available reactive groups per protein (DG). Protein reactivity, described by the DG max and initial speed of glycation (v), followed the same order for each protein-saccharide incubation: α-lactalbumin > β-lactoglobulin ≫ β-casein. Glycation of whey proteins by different monosaccharides was double that of β-casein. Differences in DG between whey proteins and β-casein decreased with increased saccharide size. A two-fold difference was found for glycation in the presence of the dimers lactose and maltose for β-casein but not for the whey proteins. The percentage of glycated lysines increased with increased lysine to protein size ratio. en application/pdf https://research.wur.nl/en/publications/maillard-induced-glycation-behaviour-of-individual-milk-proteins 10.1016/j.foodchem.2018.01.106 https://edepot.wur.nl/441633 Reactivity α-Lactalbumin β-Casein β-Lactoglobulin https://creativecommons.org/licenses/by-nc-nd/4.0/ Wageningen University & Research
institution WUR NL
collection DSpace
country Países bajos
countrycode NL
component Bibliográfico
access En linea
databasecode dig-wur-nl
tag biblioteca
region Europa del Oeste
libraryname WUR Library Netherlands
language English
topic Reactivity
α-Lactalbumin
β-Casein
β-Lactoglobulin
Reactivity
α-Lactalbumin
β-Casein
β-Lactoglobulin
spellingShingle Reactivity
α-Lactalbumin
β-Casein
β-Lactoglobulin
Reactivity
α-Lactalbumin
β-Casein
β-Lactoglobulin
Cardoso, Hugo B.
Wierenga, Peter A.
Gruppen, Harry
Schols, Henk A.
Maillard induced glycation behaviour of individual milk proteins
description This paper set out to differentiate the Maillard induced glycation reactivity of individual milk proteins using different saccharides under well-defined reaction conditions. α-Lactalbumin, β-lactoglobulin and β-casein were incubated with mono-, di- and trisaccharides in the dry state under standardised buffered conditions and glycation was expressed relative to the available reactive groups per protein (DG). Protein reactivity, described by the DG max and initial speed of glycation (v), followed the same order for each protein-saccharide incubation: α-lactalbumin > β-lactoglobulin ≫ β-casein. Glycation of whey proteins by different monosaccharides was double that of β-casein. Differences in DG between whey proteins and β-casein decreased with increased saccharide size. A two-fold difference was found for glycation in the presence of the dimers lactose and maltose for β-casein but not for the whey proteins. The percentage of glycated lysines increased with increased lysine to protein size ratio.
format Article/Letter to editor
topic_facet Reactivity
α-Lactalbumin
β-Casein
β-Lactoglobulin
author Cardoso, Hugo B.
Wierenga, Peter A.
Gruppen, Harry
Schols, Henk A.
author_facet Cardoso, Hugo B.
Wierenga, Peter A.
Gruppen, Harry
Schols, Henk A.
author_sort Cardoso, Hugo B.
title Maillard induced glycation behaviour of individual milk proteins
title_short Maillard induced glycation behaviour of individual milk proteins
title_full Maillard induced glycation behaviour of individual milk proteins
title_fullStr Maillard induced glycation behaviour of individual milk proteins
title_full_unstemmed Maillard induced glycation behaviour of individual milk proteins
title_sort maillard induced glycation behaviour of individual milk proteins
url https://research.wur.nl/en/publications/maillard-induced-glycation-behaviour-of-individual-milk-proteins
work_keys_str_mv AT cardosohugob maillardinducedglycationbehaviourofindividualmilkproteins
AT wierengapetera maillardinducedglycationbehaviourofindividualmilkproteins
AT gruppenharry maillardinducedglycationbehaviourofindividualmilkproteins
AT scholshenka maillardinducedglycationbehaviourofindividualmilkproteins
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