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Extraction and Characterization of Surfactants from Atmospheric Aerosols
Published on: April 21, 2017
Protein recovery from surfactant precipitation
Shu Ian Cheng1, David C Stuckey
1Dept. of Chemical Engineering and Chemical Technology, Imperial College London, London, UK.
Biotechnology Progress
|January 12, 2012
Summary
Researchers recovered lysozyme using solvents or a counterionic surfactant. The counterionic surfactant method achieved 100% recovery, preserving enzyme activity and structure.
Area of Science:
- Biochemistry
- Protein Chemistry
- Separation Science
Background:
- Lysozyme recovery from solutions with precipitated complexes is challenging.
- Surfactant precipitation can lead to protein loss and denaturation.
- Efficient and stable protein recovery methods are crucial for biotechnological applications.
Purpose of the Study:
- To investigate methods for recovering lysozyme from sodium bis-(2-ethylhexyl) sulfosuccinate (AOT) precipitates.
- To evaluate the efficiency and impact on protein stability of different recovery techniques.
- To explore the use of counterionic surfactants for enhanced lysozyme recovery.
Main Methods:
- Precipitation of lysozyme using sodium bis-(2-ethylhexyl) sulfosuccinate (AOT).
- Recovery using organic solvents (ethanol, methanol) and solvent mixtures.
- Recovery using a counterionic surfactant, tri-octylmethylammonium chloride (TOMAC).
- Analysis of recovery efficiency, protein stability, secondary structure (Circular Dichroism), and biological activity.
Main Results:
- Organic solvents dissolved AOT precipitates, recovering solid lysozyme with variable efficiency and stability.
- Counterionic surfactant (TOMAC) successfully displaced AOT, releasing lysozyme into solution.
- Complete (100%) lysozyme recovery was achieved at a 2:1 TOMAC:AOT molar ratio.
- Recovered lysozyme retained its original biological activity and secondary structure.
Conclusions:
- Counterionic surfactant-mediated recovery offers a highly efficient method for lysozyme.
- This method preserves the structural integrity and biological function of lysozyme.
- The findings provide a valuable approach for enzyme recovery in biochemical processes.
