Porous structure and adsorption properties of a hydrophobic interaction chromatography adsorbent, Sartobind Phenyl (TM), were studied using bovine gamma-globulin, lysozyme, human immunoglobulin G, ovalbumin, bovine serum albumin, and alpha-chymotrypsinogen A as tested proteins and ammonium sulphate as a kosmotropic salt promoting hydrophobic interactions. Dynamic experiments carried out in a laboratory membrane module showed that the dynamic binding capacity was independent of the flow velocity in the range of 3-45 cm/h but it increased exponentially with the salt concentration in the range of 0.5-1.5 M. A micromembrane chromatography module was used to examine the effect of pH on the binding capacity of the hydrophobic membrane. Adsorption equilibria were measured using a static batch method for all proteins but alpha-chymotrypsinogen A. The Langmuir exponential isotherm was employed to describe the effects of ammonium sulphate and protein concentrations on the adsorbed amount. (C) 2013 Elsevier B.V. All rights reserved.