Interactions among protein molecules in freeze-gel of soymilk and protein structures in heated soymilk during cooling.
To estimate the interactions forming in soymilk freeze-gel, lyophilized gel was extracted successively with various solvents. A mixture of urea, sodium dodecyl sulfate (SDS), and 2-mercaptoethanol (2-ME) dissolved the proteins effectively. The thiol-disulfide exchange reactions and hydrophobic interactions were shown to have a complex relation with a three-dimensional network. The addition of SDS or 2-ME resulted in an incomplete gel or no precipitation of soymilk. In our previous paper (Shimoyamada et al. Food Sci. Technol. Res. 1999, 5, 284-288), the significance of precooling to form small, homogeneously distributed ice crystals in soymilk was reported. In this study, precooling was shown to maintain the partially denatured structures of soybean proteins in soymilk that had unfolded due to heat treatment. These phenomena were considered to be other important functions of precooling in freeze-gelation.
Shimoyamada
M
M
Laboratory of Food Material Engineering, Faculty of Agriculture, Gifu University, 1-1 Yanagido, Gifu 501-1193, Japan.
Tômatsu
K
K
Oku
S
S
Watanabe
K
K
D000818:Animals; D003080:Cold Temperature; D005612:Freeze Drying; D006358:Hot Temperature; D008892:Milk; D008894:Milk Proteins / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013025:Glycine max
D008894:Milk Proteins