Abstract
Fluorescence spectroscopy, transmission electron microscopy (TEM), scanning electron microscopy (SEM), nuclear magnetic resonance (NMR), and differential scanning calorimetry (DSC) were used to investigate the aggregation behaviour of casein hydrolysates at three pHs (2.0, 7.0 and 10.0). A three-dimensional macroaggregate network was formed via the association of globular aggregates at pH 2.0 and 7.0. However, the degree of association of globular aggregates was low at pH 10.0. The nanostructure was more compact at pH 2.0 and looser at pH 10.0. Furthermore, studies with a pyrene probe indicated that casein enzymatic hydrolysate (CEH) aggregates may represent viable vehicles to sequester hydrophobic, insoluble organic molecules.
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