The effect of hydration and temperature on the low-frequency dynamics of the enzyme Pig liver esterase has been investigated with incoherent neutron scattering experiments. The results suggest that at low temperature, increasing hydration results in lower flexibility of the protein. At higher temperatures, systems containing sufficient number of water molecules interacting with the protein exhibit increased flexibility. The environmental force constants indicate that the environment of the protein is more rigid below than it is above the dynamical transition temperature.