Protein extraction and activity in reverse micelles of a nonionic detergent.
We describe, for the first time, the ability of a polyoxyethylene sorbitan trioleate-isopropanol microemulsion in hexane to solubilize pure proteins. The dependences of cytochrome c extraction and buffer solubilization by the reverse micellar system on ionic strength of the aqueous phase, detergent concentration, and cosurfactant concentration result in increased extraction. In addition, subtilisin (a serine protease) is shown to be active in this microemulsion. Further the activity of the enzyme can be regulated by the water content of the micelles, enabling control of enzyme activity by "solvent engineering."
Ayala
G A
GA
Department of Chemical Engineering, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, USA.
Kamat
S
S
Beckman
E J
EJ
Russell
A J
AJ