Title:Spectrometric, Thermodynamic, pH Metric and Viscometric Studies on the Binding of TEALS as Surfactant with Albumin as Biopolymer
VOLUME: 10 ISSUE: 1
Author(s):Shveta Acharya and Arun Kumar Sharma*
Affiliation:Department of Chemistry, Govt. College, Kota-324001, Rajasthan, Department of Chemistry, Govt. P.G. College, Jhalawar- 326001, Rajasthan
Keywords:Egg-protein, equilibrium dialysis, gibbs free energy, scatchard plots, surfactants, TEALS,
albumin, biopolymer.
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.
