BINDING ANALYSIS OF INTERACTION OF ALLURA RED WITH BSA PROCESS USING BINDING CAPACITY CONCEPT

Interaction of Allura Red AC with Bovine Serum Albumin (BSA) in 5mM phosphate buffer,pH=7 was studied by absorption spectroscopy. The binding isotherm, binding capacity and Scatchard plots were ploted at various temperatures. The binding constant obtained from the absorption titration data gives a binding constant of 3.38 at 25º C. The thermodynamic parameters such as binding free energy,binding enthalpy and binding enthalpy changes was calculated. The Positive value of H, Positive value of S and the negative value of G indicated that in interaction of Allura Red AC with BSA the driving force agent is entropy and this interaction is a hydrophobic interaction.