M.S. Chemical Engineering
Henry M. Rowan College of Engineering
Cytochrome c and DsRed2 were successfully extracted into reverse micelles by the contacting of an aqueous protein-containing phase with an organic phase. Two important properties that differentiate the extraction profiles of these proteins are pI and size. Cytochrome c is a relatively small, monomeric protein with a pI of 10.6. It was easily extracted into reverse micelles with the anionic surfactant AOT. DsRed2, however, is a large tetramer with a p1 of 6.3. It could not be extracted into AOT, but was extracted with the cationic surfactant CTAB, and with a wider error range than cytochrome c. CD data indicate the secondary structure of the proteins may change with solubilization into reverse micelles, despite absorption interference from the micelles. The results of this thesis suggest that extraction of certain proteins into reverse micelles is a viable primary separation step for the recombinant biotechnology industry. However, each process will have to be optimized to the protein of interest, as protein extraction is specific to certain properties and is extremely sensitive.
Baker, Michelle, "The extraction of Cytochrome C and DsRed2 into reverse micelles" (2009). Theses and Dissertations. 202.