Sharif Digital Repository

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, β-lactoglobulin and β-casein, adsorb already remarkably at much lower concentrations, i.e. less than 1. μmol/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... 

The influence of the addition of the nonionic surfactants C12DMPO, C14DMPO, C10OH, and C10EO5 at concentrations between 10-5 and 10-1 mmol/L to solutions of β-casein (BCS) and β-lactoglobulin (BLG) at a fixed concentration of 10-5 mmol/L on the dilational surface rheology is studied. A maximum in the viscoelasticity modulus |E| occurs at very low surfactant concentrations (10-4 to 10-3 mmol/L) for mixtures of BCS with C12DMPO and C14DMPO and for mixtures of BLG with C10EO5, while for mixture of BCS with C10EO5 the value of |E| only slightly increased. The |E| values... 

With modified measuring procedure and measuring cell design in the drop profile tensiometer PAT, it became possible to study the rate of water evaporation through adsorbed or spread surface layers. This method was employed to measure the rate of water evaporation from drops covered by adsorbed layers of some proteins and surfactants, in particular n-dodecanol. It was shown that the formation of dense (double or condensed) adsorbed layers of protein and the formation of 2D-condensed n-dodecanol layer decrease the water evaporation rate by 20-25% as compared with pure water. At the same time, the adsorbed layers of ordinary surfactants (sodium dodecyl sulfate and nonionic ethoxylated...