Abstract: Competitive adsorption isotherm data for two enantiomers of tryptophan, in which the stationary phase was silica-immobilized bovine serum albumin(BSA) and the mobile phase was a phosphate buffer,were measured by using the inverse method.The competitive bi-Langmuir isotherm model(Fisher coefficient is 1769.07, R²=0.9997) and equilibrium-dispersive model were selected by comparison of the experimental results and the interaction mechanism.The corresponding parameters were obtained by simulating the chromatogram of racemic mixture at 2×10^-4 mol•L^-1 and 10^-3 mol•L^-1.The results showed good agreement between the isotherm determined by the inverse method and the adsorption data (Fisher coefficient is 119.32, R²=0.9973) which confirmed the validity of the model selected.