Protein extraction using the sodium bis(2-ethylhexyl) phosphate (NaDEHP) reverse micellar system
1Department of Chemical Engineering, University of Michigan, Ann Arbor, Michigan 48109, USA.
Biotechnology and Bioengineering
|April 20, 1996
Summary
This study demonstrates an efficient liquid-liquid extraction method for proteins using a sodium bis(2-ethylhexyl) phosphate (NaDEHP) reverse micellar system. Proteins are solubilized and then recovered with high efficiency by destabilizing the micelles with divalent cations.
Area of Science:
- Biochemistry
- Separation Science
- Chemical Engineering
Background:
- Liquid-liquid extraction is crucial for protein purification.
- Reverse micellar systems offer unique solubilization properties.
- Efficient separation of proteins from surfactants remains a challenge.
Purpose of the Study:
- To investigate the extraction of cytochrome-c and alpha-chymotrypsin using a NaDEHP reverse micellar system.
- To optimize protein solubilization by adjusting pH and ionic strength.
- To develop a method for efficient protein recovery from the micellar phase.
Main Methods:
- Utilized a sodium bis(2-ethylhexyl) phosphate (NaDEHP)/isooctane/brine reverse micellar system.
- Varied aqueous phase pH and NaCl concentration to study protein solubilization.
- Employed divalent cations (e.g., Ca2+) to destabilize reverse micelles for protein release.
Main Results:
- Achieved high yield protein extraction into the NaDEHP micellar phase at neutral pH and low ionic strength.
- Demonstrated successful protein recovery by destabilizing reverse micelles with divalent cations.
- Showcased high overall efficiencies in separating proteins from the surfactant.
Conclusions:
- The NaDEHP reverse micellar system provides an effective method for protein liquid-liquid extraction.
- Protein recovery is efficiently achieved through micellar destabilization.
- This technique offers a promising approach for protein purification and separation.
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