The thermal behaviors of pore water were studied by adiabatic calorimetry between 50 and 300K. We utilized pore water in 1) silica MCM-41 with pore diameters of 1.5 to 5.0nm, 2) sephadex G10 of a cross-linked dextran gel, and 3) bovine serum albumin (BSA) of a globular protein. The three pore walls differed in hydrophilic/hydrophobic properties, pore size and shape, and flexibility. The hydration levels for G10 and BSA were h=0.273 and 0.321, as evaluated by the mass ratio of water to anhydride. Pore water in MCM-41 revealed glass transitions at around 115, 165, and 210K; the first was attributed to the freezing-in of interfacial water molecules neighboring the pore walls. The temperatures, which increased discretely with pore size, were interpreted to correspond, respectively, with the situations where 2, 3 and 4 hydrogen bonds are broken simultaneously in the activation for rearrangement of water molecule. The glass transitions in hydrated G10 and BSA displayed some similar behaviors as those in MCM-41. It was found that the number of accessible microscopic states of pore water in G10 was small with regard to the configurational degree of freedom below 273K, as compared with those of bulk water and pore water in MCM-41. The number of pore water in BSA was further small, even at 300K, suggesting that the structure of BSA with h=0.321 is determined by BSA itself and most water molecules are confined to narrow spaces.