CALORIMETRIC AND FTIR-SPECTROSCOPIC STUDY OF SOLVENT EFFECT ON THE STATE OF DRY SOLID BOVINE PANCREATIC -CHYMOTRYPSIN IMMERSED IN ANHYDROUS ORGANIC SOLVENTS

on the protein structure and thermodynamic state the solvents could be divided into two groups. The rst group exhibiting nearly zero eects consists of carbon tetrachloride, benzene, nitromethane, acetonitrile, 1,4-dioxane, n-butanol, n-propanol and pyridine. Dry solid protein is suggested to be stable in such media due to kinetic reasons. Immersion of the protein into a second group solvents, namely, dimethyl sulfoxide, methanol, ethanol, and in pure water as well, is followed by swelling of the protein and accompanied with signicant exothermic enthalpy change and structural rearrangements. It was shown that attribution of the solvent to the rst or the second group is determined by its thermodynamic hydrophilicity (partial excess molar Gibbs free energy of water in a given solvent at innite dilution). The rst group consists of liquids with thermodynamic hydrophilicities all above 2.7 kJ/mol. The thermodynamic hydrophilicities of the second group solvents are lower than 2.3 kJ/mol. At close hydrophilicities the presence of mobile protons in the solvent molecule suciently accelerates the solid protein swelling. It is deduced that thermodynamic hydrophilicity and proton donating ability could be principal factors controlling the stability of dry solid proteins and kinetics of swelling in liquids examined at room temperature.