Cu2+-attached pumice particles embedded composite cryogels for protein purification.

In this study, chromatographic performance of Cu2+-attached pumice particles embedded to monolithic cryogels (Cu2+-APPsEMC) for human serum albumin (HSA) was investigated. Monolithic composite cryogels were prepared by means of polymerization of gel-forming precursors at sub-zero temperatures. The chemical composition of pumice and surface of composite cryogels were determined by X-ray fluorescence spectrometer and scanning electron microscopy, respectively. The highest adsorption capacity (549.5 mg/g pumice) of cryogels was achieved at phosphate buffer of pH 8.0 with initial HSA solution of 3 mg/ml. SDS-PAGE analysis was performed for the samples studied on human serum to determine HSA adsorption/desorption performance of cryogel qualitatively.