The enriching mechanism of water-soluble proteins in continuous foam separation was studied. The liquid flow rate and the protein concentration in foam phase were measured at various heights from the interphase between bulk liquid and foam layer, and the intrinsic values at the interface were estimated by the extrapolation method to determine the accurate adsorption density on bubble surface. Ovalbumin (OA) and hemoglobin (HB) were used as the soluble proteins. The solution pHs were varied from 3.5, 4.6 and 6.0 for OA and from 6.0, 6.8 and 8.0 for HB. The experimental isotherms for OA and HB were compared to the Langmuir isotherm, and the two adsorption parameters of the equilibrium constant, K, and the saturated density, γ, at each pH were determined. Both γ values obtained for OA and HB showed maxima at their isoelectric point (i.e.p., pH 4.6 for OA and pH 6.8 for HB). Assuming that OA and HB molecules are spherical in shape and they are adsorbed on bubble surface in a closed packed structure at the saturated condition, the calculated diameters for OA and HB molecules were quite similar to the literature values. The variation in γ for both OA and HB were discussed qualitatively relating to the net charge of protein molecule.2