| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 602546 | Colloids and Surfaces B: Biointerfaces | 2009 | 6 Pages |
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.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Colloid and Surface Chemistry
Authors
Takayuki Y. Nara, Hideaki Togashi, Chisato Sekikawa, Masayuki Kawakami, Nakatsugu Yaginuma, Kengo Sakaguchi, Fujio Mizukami, Tatsuo Tsunoda,