Near-Infrared Spectroscopy Study of Heat-Induced Gelation and Hydration of Bovine Serum Albumin in Aqueous Solution

摘要

We calculated the activation energy for water in the process of the heat-induced gelation of bovine serum albumin (BSA) in aqueous solution. The activation energy for weakly hydrogen-bonded water and that for strongly hydrogen-bonded water were 121 kcal/mol and 52.5 kcal/mol, respectively. In the gelation, water molecules are confined in the network of the gel. Thus it may be considered that the activation energy for water is attributed to the effect of confinement in the gelation. The difference in the activation energy between weakly hydrogen-bonded water and strongly hydrogen-bonded water is considered to be attributed to the difference in the interaction with the protein molecules between both kinds of water molecules.