The influence of ethylene glycol (EG) on the kinetics of hydrolysis of N-alpha-benzoyl-L-arginine ethyl ether catalyzed by trypsin encapsulated in sodium bis-(2-ethylhexyl)sulfosuccinate (AOT)-based reverse micelles was studied at different temperatures. Ethylene glycol was shown to shift the range of the trypsin activity in the reverse micelles towards higher temperatures. Infrared spectroscopy showed a stabilizing effect of EG on the secondary structure of the protein in the system of reverse micelles. Electron spin resonance spectroscopy showed that the solubilized protein affected the interactions of EG with the polar head groups of AOT and altered the rigidity of the micellar matrix. The results indicate that EG increases the thermostability of the solubilized enzyme in microemulsion media by two mechanisms.

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Membranostabilizing effect of CAPAH is demonstrated in vivo and in vitro. The preparation decreases experimental osmotic hemolysis and prevents elevation of blood enzymes in rats exposed to hypoxia. Infrared spectroscopy and electron paramagnetic resonance show that CAPAH is located in the superticial hydrophilic layer of modeled phosphatidylcholine membranes and interacts with lipid molecules.

The effect of the sign and value of the charge of the interphase surface on the catalytic activity of trypsin in systems of inverted mycelles was investigated. n-Butanol was used for the modification of the phase interface in dispersions of inverted mycelles based on anionic sodium bis(2-ethylhexyl)sulfosuccinate (AOT) and cationic cetyltrimethylammonium bromide (CTAB). A direct correlation between changes in the state of inverted mycelles and the structure of solubilized enzyme under the action of butanol was obtained. It was shown that the enzyme activity is determined by the quantity of butanol solubilized by the inverted mycelles.