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.
Main Authors: | , , , |
---|---|
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 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
id |
dig-wur-nl-wurpubs-533901 |
---|---|
record_format |
koha |
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 |
_version_ |
1813197937020239872 |