Abstract
Water and protein dynamics in two globular protein-water systems, water-lysozyme
and water-BSA (bovine serum albumine), were studied by differential scanning calorimetry (DSC), dielectric relaxation spectroscopy (DRS) and thermally stimulated depolarization currents (TSDC) techniques. Water equilibrium sorption isotherms (ESI) measurements were also recorded at room temperature. The samples covered a wide range of composition, from practically dry solid pellets (2wt% of water) to dilute solutions (82wt% of water). Crystallization and melting events of water were studied by DSC and the amount of uncrystallized water was calculated. The evolution of dynamics with hydration level was followed for various dielectric relaxation processes, the emphasis being given to relaxation processes of polar groups on the surface of the proteins and of uncrystallized water molecules. A relationship between the formation of a conductive percolating water cluster and the saturation of the water process was found.
