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Partitioning of proteins in dextran/hydrophobically modified dextran aqueous two-phase systems
M Lu1, G Johansson, P A Albertsson
1Department of Biochemistry, University of Lund, Sweden.
Bioseparation
|January 1, 1995
Summary
Hydrophobically modified dextran polymers create aqueous two-phase systems for protein partitioning. Salt addition significantly impacts protein separation based on net charge and Hofmeister series effects.
Area of Science:
- Biochemistry
- Polymer Science
- Separation Science
Background:
- Aqueous two-phase systems (ATPS) are widely used for bioseparation.
- Hydrophobically modified dextrans offer tunable properties for ATPS design.
Purpose of the Study:
- To investigate protein partitioning in ATPS using dextran and hydrophobically modified dextrans.
- To determine the influence of salts on protein partitioning in these systems.
Main Methods:
- Preparation of benzoyl dextran (DS 0.17) and valeryl dextran (DS 0.20).
- Determination of phase diagrams for dextran/modified dextran systems.
- Measurement of protein partition coefficients (beta-galactosidase, BSA, beta-lactoglobulin, lysozyme, myoglobin, cytochrome C).
- Analysis of salt effects on protein partitioning in dextran/benzoyl dextran systems.
Main Results:
- Phase diagrams were established for the studied ATPS.
- Protein partitioning was significantly affected by the addition of salts.
- The observed salt effects correlated with protein net charge and ion-specific effects (Hofmeister series).
- Cross-partitioning behavior of bovine serum albumin was characterized.
Conclusions:
- Hydrophobically modified dextran-based ATPS provide effective platforms for protein separation.
- Salt manipulation offers a powerful strategy to control protein partitioning in ATPS.
- Understanding ion-specific effects is crucial for optimizing protein separation in these systems.