Al. Riblett et al., Characterization of beta-conglycinin and glycinin soy protein fractions from four selected soybean genotypes, J AGR FOOD, 49(10), 2001, pp. 4983-4989
The beta -conglycinin and glycinin fractions of soy protein were isolated f
rom Macon, Ohio FG1, Enrei, and IL2 genotypes that were grown under the sam
e environmental conditions. The soy protein fractions were evaluated to det
ermine whether chemical composition and gel-forming properties were related
. Amino acid analyses suggested that the hydrophobic residues may be the pr
imary cause of differences in soy protein gel characteristics as the storag
e moduli increased with higher percentages of hydrophobic residues. Reverse
d-phase high-performance liquid chromatography profiles revealed variations
in the composition of each fraction that corresponded to differences obser
ved among the storage moduli. The gel-forming properties may be related to
more than just protein content, such as the amount and type of amino acid i
n the fraction.