Protein partitioning in PEG/dextran aqueous two-phase systems
β Scribed by Alan D. Diamond; James T. Hsu
- Publisher
- American Institute of Chemical Engineers
- Year
- 1990
- Tongue
- English
- Weight
- 741 KB
- Volume
- 36
- Category
- Article
- ISSN
- 0001-1541
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π SIMILAR VOLUMES
Protein partitioning in aqueous two-phase systems based on phase-forming polymers is strongly affected by the net charge of the protein, but a thermodynamic description of the charge effects has been hindered by conflicting results. Many of the difficulties could be because of problems in isolating
During recombinant E. coli fermentation with high-expression levels inclusion bodies are often formed. Aqueous two-phase systems have been successfully used in the presence of urea for the initial recovery step of inclusion bodies from E. coli. Basic studies of the complex interactions are lacking.
## Abstract In order to develop an aqueous twoβphase system (ATPS) for cephalexin synthesis with extractive bioconversion, the partitioning behaviour of cephalexin and 7βaminodeacetoxicephalosporanic acid (7βADCA) in poly(ethylene glycol) (PEG)/salt ATPS were examined. Parameters such as PEG size,
Phase diagram data at 4Β°C was determined for the aqueous two-phase systems composed of polyethylene glycol, dextran, and water. The Flory-Huggins theory of polymer thermodynamics was used to correlate partitioning of biomolecules in these aqueous two-phase systems resulting in a simple linear relati