Nonlinear dilatational rheology of different protein aggregates at the oil-water interface

Proteins tend to self-assemble into different morphological aggregates such as nanoparticles or fibrils during heat treatment depending on the processing conditions. The protein aggregates exhibit excellent interfacial activity and even better ability to stabilize emulsions than native proteins. The interfacial rheological properties at the oil-water interface play a very important role in emulsion stability, among which the interfacial nonlinear rheology is closely related to their ability to resist large perturbation. However, there are very few studies reporting the nonlinear interfacial rheological behavior of protein aggregates at the oil-water interface. In this study, beta-lactoglobulin fibrous aggregates (F) and nanoparticle aggregates (NP) were prepared, and the adsorption kinetics and dilatational nonlinear rheological behavior of beta-lactoglobulin aggregates at the oil-water interface under large amplitude deformation were studied using a pendant drop tensiometer, and compared with those of native proteins. From the adsorption experiments, the adsorption of protein aggregates, especially fibrils, was faster than that of native proteins in the early stage, while in the late stage, the native proteins displayed a significantly higher degree of rearrangement than the fibrils. The surface hydrophobicity and the short fibrils present mainly determine the properties of the fibril interface, while the behavior of the nanoparticle interface was significantly influenced by the size and charge properties of the nanoparticles. From the dilatational experiment, the Lissajous plots revealed that the F interface at all pHs evaluated and the beta lg interface at pH 5.8 displayed strain softening in both expansion and compression processes, while the NP interface at all pHs and beta lg interface at pH 2 and pH 7 displayed strain softening in expansion and strain hardening in compression processes. The nonlinear response of the protein aggregates at the oil-water interface was more obvious at pH 5.8. The modulus change from frequency sweeps revealed that the fibril interface was strong but not very structured in contrast to that formed by the native proteins which displays high structuration although weak in strength, whereas the strength of the interface formed by protein nanoparticles is in between, but more sensitive to the surface charge.