Cryoenzymology in aqueous media: Micellar solubilized water clusters

Abstract
Amphiphilic compounds dissolved in nonpolar organic solvents formed inverted micelles whose aqueous centers can solubilize relatively large amounts of enzymes. The solutions were homogeneous and optically transparent and had low viscosity and freezing points. They provided unique and favorable systems to perform the main cryoenzymologic studies previously carried out in mixed solvents. The preparation and properties of such micelles were described. The absorbance spectra of cytochrome c at various temperatures from -38.degree. C to 20.degree. C were given. The pH dependence of trypsin-catalyzed hydrolysis of benzoylarginine ethyl ester in inverted micelles, as well as kinetic properties and activation energy, was described. Some problems were analyzed.