Related Experiment Video
Updated: Mar 12, 2026

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Hydrated ionic liquids as a liquid chaperon for refolding of aggregated recombinant protein expressed in Escherichia
K Fujita1, M Kajiyama1, Y Liu2
1Department of Biotechnology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan and Functional Ionic Liquid Laboratories (FILL), Graduate School of Engneering, Tokyo University of Agriculture and Technology, Japan.
Abstract:
We have succeeded in refolding of aggregated recombinant protein from Escherichia coli in hydrated ionic liquids. In cholinium dihydrogen phosphate containing a limited amount of water molecules, aggregated solid cellulase was dissolved and refolding was successfully carried out without further processing.
More Related Videos
08:32Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
Published on: October 23, 2016
06:30Efficient Purification of Elastin-Like Polypeptides (ELPs) from E. coli Using an Organic Solvent-based Extraction and Precipitation Method
Published on: January 9, 2026
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Ion-Exchange Chromatography