A peanut-like hollow silica (denoted as p-l-hSiO2) adsorbent is prepared in a facile method, which is composed of several silica nanospheres and has an average diameter of 22 nm, with thickness of 5 nm. Its Brunauer–Emmett–Teller (BET) surface area, pore volume and pore size are 258.9 m2 g−1, 1.56 cm3 g−1 and 3.9 nm, respectively. Then the afforded p-l-hSiO2/GSH adsorbent is applied to purify glutathione S-transferases-tagged (denoted as GST-tagged) proteins. It is found that the p-l-hSiO2 adsorbent exhibits a specific adsorption, a high binding capacity (6.80 mg g−1), good recycling performance and high recovery (90.1%) to the target proteins, showing promising potential for the affinity separation of GST-tagged proteins.
