Lysozyme kinetics in low water activity media. A possible hydration memory.
The influence of water activity on initial lysozyme kinetics is studied. Enzyme catalytic capacity exponentially increases with thermodynamical water activity of the reactant medium; this relation seems independent of the chemical structure of the water activity depressors but dependent on the structuration of water molecules they induce. This influence of water organization on initial enzyme activity is immediate and may be preserved even after a large dilution, thus lysozyme presents a "hydration memory" phenomenon. This effect is in accordance with sorption/desorption isotherms, an hysteresis loop being observed.