Abstract
Tobacco plants have the potential to be used for the production of proteins for pharmaceutical applications. This work describes a novel protein recovery strategy where the protein of interest is "tagged" with a histidine sequence, which forms a complex with cobalt ions and surfactant possessing a chelating functionality, such that the protein is recovered in the foamate of a foam fractionation step. His-gus, a histidine-tagged enzyme, was chosen as a model protein to study the feasibility of this strategy. The His-gus is recovered from spiked prefoamed tobacco extract by foam fractionation in the presence of surfactant and cobalt ions with an enrichment of 1.29 and a recovery of 21.5% in terms of an adjusted activity.
| Original language | English |
|---|---|
| Pages (from-to) | 680-2 |
| Number of pages | 3 |
| Journal | Biotechnology Progress |
| Volume | 19 |
| Issue number | 2 |
| DOIs | |
| State | Published - 2003 |
Keywords
- Chemical Fractionation/methods
- Enzyme Activation
- Feasibility Studies
- Glucuronidase/biosynthesis
- Histidine/chemistry
- Plant Extracts/chemistry
- Plant Leaves/chemistry
- Protein Binding
- Recombinant Fusion Proteins/biosynthesis
- Surface-Active Agents/chemistry
- Tobacco/chemistry
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