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Updated: Jun 28, 2026

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Use of zeolite to refold a disulfide-bonded protein
Takayuki Y Nara1, Hideaki Togashi, Chisato Sekikawa
1Research Center for Compact Chemical Process, AIST, Central 5, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8565, Japan.
Abstract:
Zeolites are microporous crystalline aluminosilicates with a highly ordered structure. Using zeolite beta as an adsorbent, denatured/reduced hen egg lysozyme was refolded to the active form at high concentrations. The denatured/reduced lysozyme was adsorbed onto the zeolite and the protein was refolded by desorbing it into refolding buffer, consisting of redox reagents, guanidine hydrochloride, polyethylene glycol, and L-arginine. This zeolite refolding method could be highly effective for various kinds of proteins, refolding them with high efficiency even when they contain disulfide bonds.
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