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Updated: Jul 14, 2026
14:25
Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Reversible folding-unfolding, aggregation protection, and multi-year stabilization, in high concentration protein
Nolene Byrne1, Li-Min Wang, Jean-Philippe Belieres
1Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, USA.
Chemical Communications (Cambridge, England)
|June 28, 2007
Summary
This study demonstrates reversible thermal unfolding and refolding of high-concentration lysozyme solutions. Ionic liquid-rich, ice-avoiding solvents stabilize proteins against aggregation and hydrolysis.
Area of Science:
- Biochemistry
- Protein Chemistry
- Materials Science
Background:
- Protein stability is crucial for applications.
- Aggregation and hydrolysis limit protein utility in solution.
- Ionic liquids offer unique solvent properties.
Purpose of the Study:
- To investigate protein behavior in novel solvent systems.
- To achieve long-term stabilization of concentrated protein solutions.
- To explore reversible thermal transitions of proteins.
Main Methods:
- Utilized high concentration (>200 mg ml(-1)) lysozyme solutions.
- Employed ionic liquid-rich, ice-avoiding solvents.
- Monitored thermal unfolding and refolding.
- Assessed stability against aggregation and hydrolysis.
Main Results:
- Achieved reversible thermal unfolding and refolding of lysozyme.
- Demonstrated long-period stabilization of lysozyme solutions.
- Prevented aggregation and hydrolysis in concentrated solutions.
- Successfully used ionic liquid-rich, ice-avoiding solvents.
Conclusions:
- Ionic liquid-rich, ice-avoiding solvents are effective for stabilizing concentrated protein solutions.
- Reversible thermal transitions are achievable under these conditions.
- This approach enhances protein utility and shelf-life.
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