Purification of Glutathione by Immobilized Metal Ion Affinity Chromatography with Thiourea as the Ligand

Immobilized metal ion affinity chromatography based on macroporous polystyrene resin was used to purify the glutathione (GSH). We found that thiourea immobilized Zn2+ has the specific capability to separate GSH. On this basis, parameters were optimized to improve both binding capacity and samples resolution. The results indicated that when the chromatography was performed with a pH 5.0 acetate buffer at a flow rate of 1 mL min−1, GSH was purified from fermentation broth with the yield of 91.22% and purity of 60.03%. Furthermore, 2 M NaCl in mobile phase can minimize non-specific interactions to improve the purity of GSH.