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Current Physical Chemistry

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ISSN (Print): 1877-9468
ISSN (Online): 1877-9476

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Research Article

Spectrometric, Thermodynamic, pH Metric and Viscometric Studies on the Binding of TEALS as Surfactant with Albumin as Biopolymer

Author(s): Shveta Acharya and Arun Kumar Sharma*

Volume 10, Issue 1, 2020

Page: [47 - 64] Pages: 18

DOI: 10.2174/1877946809666190913182152

Abstract

Background: Since the interactions of small anions with protein are very important in their transportation and distribution processes in biological systems, it is helpful to study these interactions to understand the nature of the transportation and distribution processes. Therefore, it is aimed to study the interaction of albumin with surfactant molecule by different physical methods.

Objective: Present work attempts to work on assessing the structure, characterization of the surfactants as TEALS (tri-ethanalamine lauryl sulphate) binding sites, with albumin involved in various process of living being are discussed.

Methods: The binding of surfactant TEALS to egg protein has been studied at different pH values and temperatures by spectrophotometric and equilibrium dialysis methods. The binding data were found to be pH and temperature dependent. The binding data studied by the absorbance method, were found approximately identical with those obtained from the equilibrium dialysis method.

Results: The association constants and the number of binding sites were calculated from Scatchard plots and found to be at maximum at lower pH and at lower temperature. The free energy of the combining sites was lowest at higher pH and highest at low pH. Therefore, a lower temperature and a lower pH offered more sites in the protein molecule for interaction with surfactant. The ΔG (free energies of aggregation) associated with the binding interaction of the surfactants and protein were calculated. The negative values of the ΔG confirm the feasibility of interaction between the surfactant and protein. All the observations recorded in this paper indicate that the TEALS has a good affinity of binding with egg protein and the number of binding sites is dependent on various physical and chemical factors.

Conclusion: On the basis of the results of the experiments which were conducted to examine the interaction between anionic surfactant and protein by measuring the various parameters of the solutions, it is concluded that the interaction of surfactant and protein gives an idea of fundamental understanding of the structure of surfactant-protein complex and their practical applications in every field.

Keywords: Egg-protein, equilibrium dialysis, gibbs free energy, scatchard plots, surfactants, TEALS, albumin, biopolymer.

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