抄録
Dynamics of hydration water of some proteins during freeze-thawing and after freeze-drying was investigated in the presence or absence of protective substances using DSC and ^1HNMR. Protein such as myosin, which is unstable against freezing and drying, has no rigid stable hydration structure and the extent of restriction of hydration water by the protein is weaker than other stable proteins. Addition of effective protectants, the number of hydration water decreased extremely and the extent of restriction increased. It seems that destruction of hydration structure by dehydration during freezing or drying is the most important mechanism of the protein denaturation. It is considered that the effective protectants, such as sugars, amino acids, polyols or surfactants, substitute for a part of of hydration water of protein and form quasi-hydration structure and protect protein agaist denaturation. The characteristic of "quasi-liquid layer" of ice particles was also discussed in relation to the properties of hydration water of protein.
