Interfacial properties of commercially available soft contact lens hydrogels were studied to understand thermodynamic phenomena of protein adsorption. Hydrogel particles ($1{ imes}1mm^2$) with varying water wettability were exposed to bovine serum albumin solutions for an hour. The remained albumin solutions were analyzed with Bradford assay method. The amount of protein adsorbed to hydrogels increased with protein solution concentrations following Langmuir isotherm. The partition coefficient ($P$) and Gibbs free energy cost of dehydrating the surface region by protein displacement upon adsorption increased with increasing hydrophilicity of contact lens. Understanding of physical chemistry in protein adsorption to contact lens materials enabled elucidating relationships between surface energy and albumin adsorption capacity.