To investigate the dielectric relaxations of ice in low-concentration protein-water mixtures, broadband dielectric spectroscopy measurements were performed on partially crystallized bovine serum albumin (BSA)-water mixtures with BSA concentrations of 1-10 wt% at temperatures in the range of 123-298 K. The temperature dependence of the relaxation time of ice observed in all these mixtures changes twice at (∼240 K) and (200-160 K) ( > ), , at which the apparent activation energy, , changes. Below 200 K, the relaxation of ice separates as 3-4 relaxations with different and values. The presence of the multiple ice relaxations is the same as that observed for the gelatin-water mixtures (T. Yasuda, K. Sasaki, R. Kita, N. Shinyashiki and S. Yagihara, , 2017, , 2896), but the concentration dependences of and are different. The relaxation interpreted to be due to uncrystallized water in 20 wt% and 40 wt% BSA-water mixtures reported (N. Shinyashiki, W. Yamamoto, A. Yokoyama, T. Yoshinari, S. Yagihara, R. Kita, K. L. Ngai and S. Capaccioli, , 2009, , 14448) was re-examined and concluded to be due to one of the multiple relaxations of ice.
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