The rheological properties of bovine β-Lactoglobulin stabilized oil/water interfaces depend on the protein's quaternary structure

Interfacial Properties of Pea Protein Hydrolysate: The Effect of Ionic Strength

“…At 0.4 M NaCl, both kp and kr decreased compared to 0.1 M NaCl. At higher salt concentrations (0.4 M NaCl), the reduction of electrostatic repulsions promotes a denser packing of protein molecules [38]. k p and k r were fitted well to the first-order equation (LR > 0.958) for all the samples with salt.…”

“…Considering the adsorption kinetics of SPPH in an oil/water interface, it can be concluded that diffusion is the main mechanism that controls protein adsorption [36]. Penetration is correlated with NaCl concentration (Table 2); however, no correlation was found between NaCl concentration and the rearrangement rate, suggesting that postadsorption changes are not influenced by ionic strength [38].…”

“…At 0.4 M NaCl, both k p and k r decreased compared to 0.1 M NaCl. At higher salt concentrations (0.4 M NaCl), the reduction of electrostatic repulsions promotes a denser packing of protein molecules [38].…”

“…The second phase includes peptide rearrangement at the interface and the formation of a monolayer. It can be identified as a steep increase of G' and a corresponding decrease of tan 𝛿 [38]. The third phase is referred to as the steady state, where G' and tan 𝛿 reach a plateau [15].…”

Porous hydrogel composite with whey protein isolate and galactomannans of Leucaena leucocephala (subabul) seeds: Stability, rheological, thermal, and morphological characterization

“…When WPI is heated near its denaturation temperature, there is a disruption of native structure to form further monomers along with secondary and tertiary structures. Heating of WPI < 65°C generates certain oligomers (Ramamirtham et al., 2021; Verheul et al., 1998), which hinders the foam formation by restricting the unfolding of the protein after diffusion to the air–water interface (Buggy et al., 2018). In contrast, at higher temperature (>65–75°C) and pH above 6, the exposed thiol groups of the monomers of β‐lactoglobulins form non‐covalent bonds that then form a gel network (Setiowati et al., 2020).…”