Abstract
The spread layers of lysozyme (LYS) microgel particles were studied by surface dilational rheology, infrared reflection-absorption spectra, Brewster angle microscopy, atomic force microscopy, and scanning electron microscopy. It is shown that the properties of LYS microgel layers differ significantly from those of ß-lactoglobulin (BLG) microgel layers. In the latter case, the spread protein layer is mainly a monolayer, and the interactions between particles lead to the increase in the dynamic surface elasticity by up to 140 mN/m. In contrast, the dynamic elasticity of the LYS microgel layer does not exceed the values for pure protein layers. The compression isotherms also do not exhibit specific features of the layer collapse that are characteristic for the layers of BLG aggregates. LYS aggregates form trough three-dimensional clusters directly during the spreading process, and protein spherulites do not spread further along the interface. As a result, the liquid surface contains large, almost empty regions and some patches of high local concentration of the microgel particles.