Staff Publications

Staff Publications

  • external user (warningwarning)
  • Log in as
  • language uk
  • About

    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

    We have a manual that explains all the features 

Record number 533901
Title Maillard induced glycation behaviour of individual milk proteins
Author(s) Cardoso, Hugo B.; Wierenga, Peter A.; Gruppen, Harry; Schols, Henk A.
Source Food Chemistry 252 (2018). - ISSN 0308-8146 - p. 311 - 317.
DOI https://doi.org/10.1016/j.foodchem.2018.01.106
Department(s) Food Chemistry Group
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2018
Keyword(s) Reactivity - α-Lactalbumin - β-Casein - β-Lactoglobulin
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.
Comments
There are no comments yet. You can post the first one!
Post a comment
 
Please log in to use this service. Login as Wageningen University & Research user or guest user in upper right hand corner of this page.