Adsorption of proteins at the solution/air interface influenced by added non-ionic surfactants at very low concentrations for both components. 1. Dodecyl dimethyl phospine oxide

作者：Lotfi M^*; Jayadi A; Lylyk S V; Bastani D; Fainerman V B; Miller R

来源：Colloids and Surfaces A: Physicochemical and Engineering Aspects , 2015, 475: 62-68.

DOI：10.1016/j.colsurfa.2014.12.065

• Adsorption of whey proteins BLG and BCS
• Dynamic surface tensions
• Addition of non-ionic surfactants
• Bubble profile analysis tensiometry
• Capillary pressure tensiometry

The adsorption of proteins at liquid interfaces happens at rather low bulk concentrations due to their rather high surface activity. In contrast typical surfactants start to decrease the surface tension at bulk concentration in the range of mmol/l and reach a minimum value at about two or three orders of magnitude higher concentration. The two proteins studied here, beta-lactoglobulin and beta-casein, adsorb already remarkably at much lower concentrations, i.e. less than 1 mu mol/l. When smallest amounts of a non-ionic surfactant are added to low concentrated protein solutions, changes in the surface tension are observed which cannot be explained by the existing theoretical models. An agreement with the experimental data can be achieved only when an increased surface activity of the protein due to the interaction with the surfactants is assumed.

• 出版日期2015-6-20