Abstract
Herein, the interaction of a protein, bovine serum albumin (BSA), with tetradecyltrimethylammonium bromide (TTAB, a cationic surfactant), has been investigated using the conductivity measurement technique in pure water and some sodium salts (NaCl, Na2SO4, Na2CO3, and Na3PO4) solutions at temperature range of 295.15–320.15 K. Results reveal that, in the plot of specific conductivity versus the concentration of TTAB, only a single critical micelle concentration (cmc) was found for the TTAB + BSA mixed system in all solvents media studied. The addition of BSA in aqueous TTAB solution, the value of cmc undergoes a change from its pure form, which indicates the presence of strong interaction operating between the BSA and TTAB molecules. In aqueous system, the cmc values of the TTAB + BSA mixtures are obtained higher compared to the values found for single TTAB surfactant. However, the addition of salt decreases the cmc value of mixed TTAB + BSA system. The values of cmc of the BSA + TTAB mixed system at 310.15 K and 1.00 mmol·kg−1 ionic strength of salt followed the order: cmcNa2CO3 > cmcNa3PO4 > cmcNaCl > cmcNa2SO4. The cmc values of TTAB + BSA mixture were found to be lowered in urea solution within the concentrations studied. The values of degree of dissociation (α) and fraction of counter ion binding (β) were found to be dependent on additives and temperature. The free energy of micellization (∆Gmo) is negative for all the systems, which manifests that the micellization phenomenon is energetically spontaneous. The enhancement of the negative value of ∆Gmo in aqueous salt solutions reveals an increase of spontaneity of the TTAB + BSA micellization process. The values of ∆Gmo also reveal that the spontaneity of micelle formation is enhanced at higher temperatures in all media studied. The values of free energy of transfer (∆Gm, to) were also determined for numerous solvent media used in the present study and described with appropriate reasoning.
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