Abstract
The study delves into the adsorption of sunflower proteins at the air/water interface using specular X-ray reflection. The research involved fitting models of the protein films to the reflectivity data, resulting in detailed images of the X-ray scattering length density profiles perpendicular to the air/water interface. The sunflower protein isolate that is examined consists of multiple components, and the study proposes a transition from a 1-slab model to a 4-slab model to represent the changing layer structure over time. This transition is significant as it reflects the increasing complexity of the protein film as more proteins adsorb at the interface. Initially, sunflower proteins form a monolayer at the air/water boundary, consisting of a protein-rich, hydrophobic portion closest to the interface and a more diffuse, hydrophilic portion extending into the bulk aqueous phase. The structural changes at the interface over time depend on the bulk protein concentration in the solution. For solutions at relatively low concentrations (C ≤ 0.5 g/L), a lower amount of adsorption results in a larger, more extensive interface area for each species and a thinner protein adsorption layer. The overall thickness of a saturated monolayer is approximately 100 Å, which is close to the maximum dimension of sunflower globulins, with the thickness of the corresponding hydrophobic portion being about 20 Å. For solutions at relatively high concentrations (C ≥ 1.0 g/L), even after forming a saturated monolayer, structural evolution continues within the experimental time frame, occurring on both hydrophilic and hydrophobic sides. Additional proteins from the bulk diffuse toward the interface, forming an extra layer in the water phase and causing an increase in the overall thickness. Furthermore, a distinct sublayer develops next to the air phase, indicating a further structuration of the hydrophobic portion.