In this study, the relationship between the deterioration of the enzymatic activity of the protein in a preservative solution and the molecular mobility of the preservative solution was experimentally investigated by dielectric spectroscopy and a protein deterioration test. Dielectric spectroscopy was used to observe the molecular mobilities in the preservative solutions including various ratios of two protective agents, trehalose and epsilon-poly-L-lysine, at 40 degrees C. We also examined the enzymatic activity of L-lactate dehydrogenase (LDH) at 40 degrees C for 40 days to obtain the deterioration rate of LDH in the same preservative solutions. Our experimental results reveal that (1) three relaxation times of water molecular motion are detected by dielectric spectroscopy that we categorize into bulky water (relaxation time of 10 ps), weakly hydration water (relaxation time of tens to hundreds of picoseconds), and strongly hydration water (relaxation time of hundreds of picoseconds to tens of microseconds) and (2) the deterioration rate of LDH has a power-law relationship with the relaxation times of bulky and hydration water with specific power indices. The results also support the protein stabilization theory of high viscosity and the practical advantage of predicting the shelf life of proteins in the preservative solution by the relaxation time of water measured by dielectric spectroscopy.