Sharif Digital Repository

The rising velocity of air bubbles in surfactant solutions is a sensitive measure for the formation of a dynamic adsorption layer (DAL) at the bubble surface. Due to a certain surface coverage by adsorbed species the bubble surface starts to become immobilized and the rising velocity is retarded. There is a large difference in the retardation effect in presence of the protein β-lactoglobulin (BLG) alone and its mixed solutions with surfactants. In presence of added surfactants BLG forms complexes, which adsorb and retard the bubble rising velocity according to their respective surface activity and adsorption kinetics. While the nonionic surfactant C12DMPO does not show significant increase... 

A computational approach to predict the main binding modes of two adrenalin derivatives, arachidonoyl adrenalin (AA-AD) and arachidonoyl noradrenalin (AA-NOR) with the β-lactoglubuline (BLG) as a nano-milk protein carrier is presented and assessed by comparison to the UV-Vis absorption spectroscopic data using chemometric analysis. Analysis of the spectral data matrices by using the multivariate curve resolution-alternating least squares (MCR-ALS) algorithm led to the pure concentration calculation and spectral profiles resolution of the chemical constituents and the apparent equilibrium constants computation. The negative values of entropy and enthalpy changes for both compound indicated... 

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... 

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 present study aimed to improve the survivability of L. acidophilus encapsulated in alginate-whey protein isolate (AL-WPI) biocomposite under simulated gastric juice (SGJ) and simulated intestinal juice (SIJ). Microcapsules were prepared based on emulsification/internal gelation technique. Optimal compositions of AL and WPI and their ratio in the aqueous phase were evaluated based on minimizing mean diameter (MD) of the microcapsules and maximizing encapsulation efficiency (EE), survivability of cells under SGJ (Viability), and release of viable cells under SIJ (Release) using Box-Behnken experimental design. Optimal composition comprising 4.54% (w/v) AL, 10% (w/v) WPI, and 10% (v/v)... 

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...