Maillard induced glycation behaviour of individual milk proteins

Hugo B. Cardoso, Peter A. Wierenga, Harry Gruppen, Henk A. Schols*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

47 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)311-317
JournalFood Chemistry
Volume252
DOIs
Publication statusPublished - 30 Jun 2018

Keywords

  • Reactivity
  • α-Lactalbumin
  • β-Casein
  • β-Lactoglobulin

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