Structure-physicochemical function relationships of soybean beta-conglycinin heterotrimers.
We purified four single molecular species of beta-conglycinin heterotrimers consisting of the alpha and beta subunits or the alpha' and beta subunits from mutant soybean cultivars lacking the alpha or alpha' subunit, respectively, and examined their structural features and physicochemical functions. The extent of the hydrophobicities of the heterotrimers was related to the number of the alpha or alpha' subunit. The thermal stabilities of the heterotrimers were mainly conferred by the subunit which had lower thermal stability. Solubilities at low ionic strength (mu = 0.08) of the heterotrimers containing the alpha or alpha' subunit were very similar to those of the alpha and alpha' homotrimers, respectively. Emulsifying abilities and heat-induced associations of the heterotrimers containing one beta subunit were similar to those of the alpha or alpha' homotrimer, whereas those of the heterotrimers containing two beta subunits were similar to those of the beta homotrimer.
Maruyama
Nobuyuki
N
Laboratory of Food Quality Design and Development, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan.
Mohamed Salleh
Mohamad Ramlan
MR
Takahashi
Koji
K
Yagasaki
Kazuhiro
K
Goto
Hideyuki
H
Hontani
Naho
N
Nakagawa
Shuko
S
Utsumi
Shigeru
S
D052179:Antigens, Plant; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004355:Drug Stability; D005079:Excipients / Q000737:chemistry; D005916:Globulins / Q000737:chemistry*; D006358:Hot Temperature; D055314:Seed Storage Proteins; D012995:Solubility; D030262:Soybean Proteins; D013025:Glycine max / Q000737:chemistry*; D013329:Structure-Activity Relationship
D052179:Antigens, Plant; D005079:Excipients; D005916:Globulins; D055314:Seed Storage Proteins; D030262:Soybean Proteins; C013894:beta-conglycinin protein, Glycine max