Maillard induced aggregation of individual milk proteins and interactions involved

•α-Lactalbumin, β-lactoglobulin and β-casein reached different heat induced aggregation extent.•The presence of glucose led to similar Maillard induced aggregation extent for the three proteins.•Protein aggregation is reduced with increasing saccharide size during Maillard reaction.•Protein disulphi...

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Bibliographic Details
Published inFood chemistry Vol. 276; pp. 652 - 661
Main Authors Cardoso, Hugo B., Wierenga, Peter A., Gruppen, Harry, Schols, Henk A.
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 15.03.2019
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Summary:•α-Lactalbumin, β-lactoglobulin and β-casein reached different heat induced aggregation extent.•The presence of glucose led to similar Maillard induced aggregation extent for the three proteins.•Protein aggregation is reduced with increasing saccharide size during Maillard reaction.•Protein disulphide bridges formation is stimulated by the Maillard reaction.•Blocking of cysteines prior to Maillard reaction increases the formation of other crosslinks. The aggregation of α-lactalbumin, β-lactoglobulin and β-casein after heating in dry state was studied in absence and presence of saccharides. In absence of saccharides, differences were observed in the extent of aggregation. Differences between the proteins were mostly due to differences in covalent aggregation. The presence of glucose during the heat treatment of milk proteins significantly increased the extent of aggregation, and decreased differences between proteins. α-Lactalbumin was selected as a model protein for the study of cross-links formed after heat treatment. In the presence of saccharides, these cross-links were found to consist of 36% of disulphide bridges (compared to >75% in the absence of glucose), followed by other cross-links such as lanthionine. Larger saccharides led to a decrease in Maillard induced aggregation; maltotriose actually even inhibited the formation of α-lactalbumin aggregates.
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ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2018.10.061