Maillard induced aggregation of individual milk proteins and interactions involved.

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.

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 and initial speed of glycation (v), followed the same order for each protein-saccharide incubation: α-lactalbumin > β-lactoglobulin ≫ β-casein.