Arginine has been shown to suppress the aggregation of proteins. Here the aquous solubility enhancement of highly insoluble protein “gluten” in presence of arginine was re-examined. Further in order to understand the thermodynamics and solute solvent interactions during the solubility enhancement of gluten in presence of arginine, the ternary system has been subjected to conductometric measurements. The conductance values have been used to evaluate the limiting molar conductance and association constants by means of Shedlovsky extrapolation technique. The thermodynamic parameters for the association process of arginine in presence of gluten in water have also been calculated. A concentration dependence solubility enhancement of gluten was observed. It was observed that, arginine enhances the solubility of gluten by 15.71 folds as compared to that in water.
Gluten, Arginine, Limiting molar conductance, Association constant