Single-solute isotherms for pepsin (EC 3.4.23.1) and chymosin (EC 3.4.23.4) adsorption to affinity membranes were fitted using five of the most popular isotherm models. It was found that the single-solute Langmuir isotherm was the best two-parameter model, although the three-parameter models gave even better fitting. Experimental binary-solute adsorption isotherms were compared with four different types of binary-solute Langmuir models using the single-solute parameters. The results showed that the difference in the saturation capacities affected the adsorption equilibrium. Furthermore, three types of binary-solute Langmuir models were converted into the kinetic form and used to calculate the association rate constants of pepsin and chymosin from experimental data. The best-fitted rate constant values were found to be identical for different kinetic models. However, the model predictions of association curves were significantly influenced when the values of association rate constants were changed.