Whey protein-based
emulsion gels were fabricated by combined covalent
cross-linking with cinnamaldehyde and ionic cross-linking with calcium
ions. The structural and rheological properties of these emulsion
gels were characterized by microscopy, macrorheometry, and microrheometry.
Soft to hard emulsion gels could be fabricated by altering the Ca2+ level. However, water separation occurred in the emulsion
gels at high calcium levels, indicating that an appropriate balance
of protein cross-linking was essential for a good functional performance
of the emulsion gels. At a constant calcium ion level, cross-linking
with cinnamaldehyde softened the texture of the emulsion gels and
reduced the level of water separation. Thermal treatment could be
used to strengthen the interaction between the whey proteins and calcium
ions, presumably due to protein unfolding and aggregation. Rheology
demonstrated that cross-linking reactions occurred between the whey
protein and cinnamaldehyde at the oil–water interface, which
decreased the viscosity of the emulsion gels, but increased their
viscoelasticity. Microstructural changes observed by fluorescence
microscopy were in agreement with the rheology results. Scanning electronic
microscopy showed that the microstructure of the emulsion gels was
strongly impacted by the presence of cinnamaldehyde, which led to
a more uniform and smaller pore size. The gastrointestinal fate of
the emulsion gels was determined using a simulated gastrointestinal
tract model. The oral and gastric processing of the emulsion gels
was strongly influenced by cinnamaldehyde cross-linking, with less
aggregation being observed. The information obtained in this study
may facilitate the development of more innovative protein-based products
with novel functional attributes for use in foods and other applications.