Thermodynamics and rheology of mixed protein–surfactant adsorption layers

The influence of size, structure and hydrophilicity of model surfactants on the adsorption of lysozyme to oil–water interface—Interfacial shear measurements

“…This may be due to the fact that the more hydrophilic surfactants are mixed with the protein prior to the exposure to the interface. Thus they may already have interacted with the protein in the bulk solution, preventing the adsorption due to the weak hydrophobic interactions between the surfactant and the protein, which would make the complex more hydrophilic and less surface active [21]. Gunning et al have found that prevention of adsorption is not influenced by the interaction between surfactant and protein [22].…”

Dilational rheology of protein films adsorbed at fluid interfaces

“…In recent years, much work has been reported on aqueous mixtures of proteins and small-area surfactants [26][27][28][29][30][31]. Many more examples could be cited, and the list is still growing.…”

Influence of Protein Type on the Antimicrobial Activity of LAE Alone or in Combination with Methylparaben

“…However, it has already been reported in other studies that hydrophobic interactions play a role in protein surfactant complex formation [27]. For instance, Miller et al [28] studied the interaction between cationic surfactants and proteins and summarized that in the presence of low surfactant concentrations the interactions with proteins are predominately due to electrostatic forces, while at high surfactant concentrations (after saturation of negative charges) hydrophobic interactions get more pronounced. In the present study, the point of saturation was only exceeded in the presence of soy protein hydrolysate, which is directly related to the difference in protein structure.…”