This research investigates the effects of clathrate hydrate formation in reversed micellar solutions on the solubility and conformation of proteins. Preliminary results show that hydrate formation can, under certain conditions, effect protein solubilization into micelles when conventional phase transfer methods prove ineffective. It has also been found that hydrate formation is a method of in-situ modification of micelle size, and thereby, of protein conformation and enzyme activity. Therefore a set of related studies is proposed that exploit these concepts to enhance protein extraction into reversed micelles, and recovery in appropriate form. The use of hydrates to alter the catalytic activity of enzymes in reversed micelles is also proposed. The phenomenon of hydrate formation in reversed micelles is essentially unstudied up to the present. To a large extent, this research is phenomenological, and certain aspects are exploratory.
