The influence of protein encapsulation in the water pool of the reverse mice|les has been studied by the electron spin resonance (ESR) spin-label technique and electrical conductivity measurements. For this purpose water-sodium-bis(2-ethylhexyl)-sulfosuccinate (AOT)-decane water-in-oil microemulsions with so|ubilized trypsin were used. The ESR data, obtained with the help of 4-(2-n-undecyl-3-oxyl-4,4-dimethyloxazolidin-2-yl) butyric acid as a label, show that the protein molecule encapsulated in the water core of a reverse micelle forces a portion of water out from the aqueous core into the hydrophobic shell of a micelle. As a result, changes in the packing of AOT hydrocarbon chains and in the polarity of their microenvironment are induced. The effect of the encapsulated protein depends on -the difference in the sizes of the protein molecule and the micelle aqueous core. The perturbations in the dynamic structure of the surfactant shell tum out to be most pronounced when the dimensions of the water cavity ate close to the size of the protein molecule. The solubilization of protein in the reverse mice|les results in remarkable va¡ in mass exchange between micelles.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.