Metal‐chelated polyamide hollow fibers for human serum albumin separation

We modified microporous polyamide hollow fibers by acid hydrolysis to amplify the reactive groups and subsequent binding of Cibacron Blue F3GA. Then, we loaded the Cibacron Blue F3GA‐attached hollow fibers with different metal ions (Cu 2+ , Ni 2+ , and Co 2+ ) to form the metal chelates. We characterized the hollow fibers by scanning electron microscopy. The effect of pH and initial concentration of human serum albumin (HSA) on the adsorption of HSA to the metal‐chelated hollow fibers were examined in a batch system. Dye‐ and metal‐chelated hollow fibers had a higher HSA adsorption capacity and showed less nonspecific protein adsorption. The nonspecific adsorption of HSA onto the polyamide hollow fibers was 6.0 mg/g. Cibacron Blue F3GA immobilization onto the hollow fibers increased HSA adsorption up to 147 mg/g. Metal‐chelated hollow fibers showed further increases in the adsorption capacity. The maximum adsorption capacities of Co 2+ ‐, Cu 2+ ‐, and Ni 2+ ‐chelated hollow fibers were 195, 226, and 289 mg/g, respectively. The recognition range of metal ions for HSA from human serum followed the order: Ni(II) > Cu(II) > Co(II). A higher HSA adsorption was observed from human serum (324 mg/g). A significant amount of the adsorbed HSA (up to 99%) was eluted for 1 h in the elution medium containing 1.0 M sodium thiocyanide (NaSCN) at pH 8.0 and 25 m M ethylenediaminetetraacetic acid at pH 4.9. Repeated adsorption–desorption processes showed that these metal‐chelated polyamide hollow fibers were suitable for HSA adsorption. © 2002 Wiley Periodicals, Inc. J Appl Polym Sci 86: 3346–3354, 2002