Abstract
The electrochemical properties of an interface between two immiscible solutions of electrolytes are investigated as the interface is altered by adsorption of the water soluble protein bovine serum albumin. Cyclic voltammetry and electrical impedance spectrum analysis are employed as the tools of this study. The impedance behavior in the presence of bovine serum albumin shows that the protein macromolecule is adsorbed at the interface. The imaginary impedance of the interface increases with increasing concentration of bovine serum albumin to about 10 ppm, suggesting that the adsorbed monolayer forms gradually, which causes the interfacial capacitance to decrease. The impedance behavior has been analyzed as a function of applied interfacial potential. The potential of zero charge of the interface was obtained for different concentrations of bovine serum albumin. The impedance behavior is further discussed as a function of pH and temperature.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
