Abstract
Thermally stimulated depolarization current measurements on hydrated solid samples of the protein casein in the temperature range 77–300 K and the water content range 1–24 % (w/w) show two dispersions, a low-temperature dispersion in the range 100–170 K, and a high-temperature dispersion in the range 190–290 K. The high-temperature dispersion was studied in detail using several experimental techniques offered by the TSDC method. It consists, for high water contents, of two complex bands numbered I and II in the order of increasing temperature. Band I is attributed to water-assisted relaxation of polar side chains ans band II to space-charge relaxation.
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