Characterization of beta-conglycinin and glycinin soy protein fractions from four selected soybean genotypes.
The beta-conglycinin and glycinin fractions of soy protein were isolated from Macon, Ohio FG1, Enrei, and IL2 genotypes that were grown under the same environmental conditions. The soy protein fractions were evaluated to determine whether chemical composition and gel-forming properties were related. Amino acid analyses suggested that the hydrophobic residues may be the primary cause of differences in soy protein gel characteristics as the storage moduli increased with higher percentages of hydrophobic residues. Reversed-phase high-performance liquid chromatography profiles revealed variations in the composition of each fraction that corresponded to differences observed 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 in the fraction.
Riblett
A L
AL
Department of Animal Sciences and Industry, Kansas State University, Manhattan, Kansas 66506-1600, USA.
Herald
T J
TJ
Schmidt
K A
KA
Tilley
K A
KA
D000596:Amino Acids / Q000032:analysis; D052179:Antigens, Plant; D002152:Calorimetry, Differential Scanning; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005782:Gels / Q000737:chemistry; D005838:Genotype; D005916:Globulins / Q000032:analysis*; D057927:Hydrophobic and Hydrophilic Interactions; D012212:Rheology; D055314:Seed Storage Proteins; D030262:Soybean Proteins / Q000737:chemistry*; D013025:Glycine max / Q000737:chemistry / Q000235:genetics*
D000596:Amino Acids; D052179:Antigens, Plant; D005782:Gels; D005916:Globulins; D055314:Seed Storage Proteins; D030262:Soybean Proteins; C013894:beta-conglycinin protein, Glycine max; C011474:glycinin