## Abstract A novel process has been developed which uses reversed micelles to isolate denatured protein molecules from each other and allows them to refold individually. These reversed micelles are aqueous phase droplets stabilized by the surfactant AOT and suspended in isoβoctane. By adjusting co
Photoreduction of protein in reverse micelles
β Scribed by M.P. Pileni
- Publisher
- Elsevier Science
- Year
- 1981
- Weight
- 77 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0047-2670
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A novel process has been developed to improve the refolding yield of denatured proteins. It uses reversed micelles to isolate denatured protein molecules from each other and thus, upon refolding, reduces the intermolecular interactions which lead to aggregation. The feasibility of this process was f
In protein extraction, using the nonionic surfactant sugar ester DK-F-110, the critical micelle concentration (CMC) of a DK-F-110/isopropyl alcohol(IPA)/hexane system was found to be at a DK-F-110 concentration of 0.5 g dm-3, indicating that the sugar ester reverse micelles could be formed in hexane