Mechanisms of Gelation for Heat-induced and Spontaneous Gels of Proteins

点击翻译按钮获取中文摘要

On the basis of the parameters obtained by dynamic viscoelastic measurement (the critical concentration of gelation and the number of segments for forming the junction zone) and calculating the intrinsic viscosity of protein dispersions, and the correlation between the parameters obtained by static viscoelastic measurement (activation energies and fractional free volumes) and microstructure of gels by microscopy were investigated the geling mechanism of heat-induced and spontaneous protein gels. It was found that; (1)formation of junction zone for heat-induced gels were largely influenced by hydrophobic interactions, (2)protein molecules possessed the large occupied volume when gels were formed, (3)junction zone of protein gels were formed by 3-4 segments and (4) SS/SH interactions and hydrogen bondings played an important role for forming the junction zone of protein gels.It was concluded that both heat-induced and spontaneous gels intrinsically possessed the same gelling mechanism, i.e., the gelling mechanism can be expressed how the water structure surrounding the proteins were changed. The water structure surrounding the protein molecules might be broken by urea in the case of spontaneous gelation and by heating in the case of heat-induced gelation.