The Interaction of surfactants to gliadin (Wheat Protein) by dialysis equilibrium method

A Study on the binding of sodium dodecyl sulphate (SDS) and sodium octyl sulphate to gliadin was made by employing dialysis equilibrium method. The binding data reveals that the rising molar concentration of the surfactants correspond to the changes in the binding process. In the lower concentration range (region A) of the surfactants, the plot VM Vs log Cf represented linear behaviour. This region was found to have maximum number of binding sites (n) available. Beyond region B, the way of binding is found to change and binding appears to be more statistical in nature. In region C of binding isotherm VM is found to increase apparently without limit. The linking is probably be much weaker in this region than the region A due to the involvement of the non-specific forces. In the region C which is the region of relatively low proportion of protein to surfactant, the value of VM increases apparently without limit and its value for exceed the number of total positively charged groups in the protein molecule. The data show that either any conformation change or binding of surfactant with gliadin gives abnormal binding isotherms.