Gelling properties of soybean beta-conglycinin having different subunit compositions.
The effects of protein concentration, and heating temperature and time on the gelling properties of soybean beta-conglycinin (7S globulins) lacking the alpha or alpha' subunit were compared with those of 7S containing all three subunits (alpha, alpha', and beta) to determine whether each subunit contributes equally. In most of the conditions, the relative order of gel hardness was alpha'-lacking > 7S > alpha-lacking. From Fourier transform infrared studies, the secondary structure change after heating was very similar among the three samples; thus, the secondary structural change is not the reason for the differences in gel hardness. By using scanning electron microscopy, we observed differences in strand thickness and the density of the gel network among the three samples. These differences correlated well with the differences in gel hardness.
Mohamad Ramlan
Bin Mohamed Salleh
BM
Laboratory of Food Quality Design and Development, Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
Maruyama
Nobuyuki
N
Takahashi
Koji
K
Yagasaki
Kazuhiro
K
Higasa
Takahiko
T
Matsumura
Yasuki
Y
Utsumi
Shigeru
S
D052179:Antigens, Plant; D005782:Gels / Q000737:chemistry; D005916:Globulins / Q000737:chemistry*; D006358:Hot Temperature; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics; D055314:Seed Storage Proteins; D030262:Soybean Proteins / Q000737:chemistry*; D013997:Time Factors
D052179:Antigens, Plant; D005782:Gels; D005916:Globulins; D021122:Protein Subunits; D055314:Seed Storage Proteins; D030262:Soybean Proteins; C013894:beta-conglycinin protein, Glycine max