Heparin-doped affinity electromembranes for thrombin purification

• Published in: Journal of membrane science Vol. 373; no. 1; pp. 89 - 97
• Main Authors: Wang, Jun, Shi, Wei, Jiang, Hairong, Wu, Guisen, Ruan, Changqing, Ge, Dongtao
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01-05-2011; Elsevier
• Subjects: adsorption; Affinity membrane; artificial membranes; Chemistry; Colloidal state and disperse state; Conducting polymers; desorption; Exact sciences and technology; General and physical chemistry; Heparin; Membranes; polymers; Polypyrrole; sorption isotherms; Surface physical chemistry; temperature; Thrombin; Conducting polymers; Affinity membrane; Thrombin; Heparin; Polypyrrole; Polymeric membrane; Elution; Purification; Porous membrane; Adsorption isotherm; Adsorption capacity; Conductivity; Polymer; Desorption; Potential; Mechanism; Protein; Adsorption; Affinity; Membrane; Models; Pyrrole polymer
• ISSN: 0376-7388; 1873-3123
• DOI: 10.1016/j.memsci.2011.02.035

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► Affinity electromembrane was fabricated using heparin as both ligand and dopant. ► Affinity electromembrane exhibited a uniform conductivity value of 1.73
×
10
−4
S/cm. ► Adsorption capacity and rate were significantly enhanced by electrical stimulation. ► Affinity electromembrane has good stability and excellent reusable performance.
Heparin-doped affinity electromembrane was fabricated by synthesizing conducting polymers polypyrrole onto porous polyethersulfone membrane using heparin as both ligand and dopant. The obtained affinity electromembrane exhibited a uniform conductivity value of 1.73
×
10
−4
S/cm. The content of heparin of affinity electromembrane was ∼0.894
mg/g membrane. Such heparin-doped affinity electromembranes were used to purify thrombin. The adsorption mechanism of thrombin and the effects of temperature, initial concentration of thrombin and potential on adsorption were investigated by batch experiments. The results showed that the adsorption capacity increased with increasing the temperature, initial concentration of thrombin and potential, and the adsorption isotherm fitted the Freundlich model well. Elution of protein showed desorption ratio was up to 93.1% using 2.0
M NaSCN solution as the desorption agent. The adsorption capacities of all the tested affinity electromembranes did not significantly change during the repeated adsorption–desorption operations.