Alteration of surface pressure of macromolecular monolayer at the air-water interface and electrochemical impedance characteristics

[Display omitted] •Langmuir isotherms of monolayer of casein & whey protein macromolecules are evaluated.•Surface pressure was altered due to intermolecular interaction of proteins.•Electrical-equivalent resistances have been identified for protein samples using EIS. Proteins are very important biological macromolecules, specific in their functions essential for many biological activities. Proteins are among the most vital components of all living matters with thousands of different types, and they are very specific in their nature which makes them important for usage in many biotechnological, biomedical, and food processing applications. Langmuir monolayer studies provide the characteristics of monolayer at the air-liquid interface. Langmuir monolayer of protein is affected by the molecular weight, macromolecular structure, denaturation and its purity. The interaction of the protein with other molecules greatly affects the behaviour of monolayer. Coconut oil layer at the air-water interface was prepared with different sub-phases including casein protein and whey protein. Wilhelmy plate measurement technique has been used to measure the surface pressure of the monolayer at the air-liquid interface. Experiments were carried out to study the stability using electrochemical impedance measurements. The electrostatic forces dominated the coconut oil - protein interaction, and the interface of macromolecules were controlled by expansion and compression. The macromolecules were adsorbed with a preferential orientation at the interface, and the stability of colloidal dispersions was governed by the intermolecular interactions. The stability using electrochemical impedance spectroscopy on the selected protein macromolecules along with other analysis were performed by varying various parameters.