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Abstract
The behavior of the dielectric properties of gelatin in the frequency range from 103 Hz to 107 Hz was investigated and compared with that of the globule protein, bovine serum albumin (BSA), desalted gelatin and BSA being used. Dielectric relaxation was observed for both the gelatin and BSA solutions. The relaxation data were fitted well by the Cole-Cole equation; the Cole-Cole parameter (β) and the relaxation time (τ) were obtained. For the BSA solutions, τ was proportional to the solution viscosity (η) at 40°C and 25°C, and the values of β at 40°C were similar to those at 25°C. For gelatin solution, τ was proportional to η at 40°C, but was not proportional to η at 25°C. In addition, the values of β at 25°C were smaller than those at 40°C. These results indicate that the rotation of gelatin and/or polarization of submolecular groups in the coil state greatly contributed to the dielectric relaxation at 40°C; on the other hand, the formation of cross-linking junctions consisting of helix structures would have affected the dielectric relaxation at 25°C.