Heat-induced Gelation of a Human Serum Albumin Solution Containing 2M Guanidine Hydrochloride(Food & Nutrition)

概要

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The temperature dependencies of the optical rotation, light transmittance and viscosity of human serum albumin (HSA) solutions containing 2 M guanidine hydrochloride were investigated, in order to elucidate the gelation mechanism. Unfolding of HSA molecules started at a certain temperature (T_d) and phase separation occurred at a higher temperature (T_s) than the T_d. The phase separation resulted in a heterogeneous, binary phase solution consisting of a fine coacervate particle phase and a dilute solution phase. At the phase separation point, there were more native state molecules than unfolded ones. No increase in viscosity was observed within the temperature range from the T_d to the T_s. An apparent increase in viscosity started at the T_s, showing that network formation proceeded from the T_s. These results suggested that the network formation was due to crosslinking among dispersed coacervate particles in the dilute solution phase.
社団法人日本農芸化学会の論文
1989-09-23