Characterization of β-Conglycinin and Glycinin Soy Protein Fractions from Four Selected Soybean Genotypes

• Published in: Journal of agricultural and food chemistry 2001-10, Vol.49 (10), p.4983-4989
• Main Authors: Riblett, Anna L, Herald, Thomas J, Schmidt, Karen A, Tilley, Kathy A
• Format: Article
• Language: English
• Subjects: Amino Acids - analysis; Antigens, Plant; Biological and medical sciences; Calorimetry, Differential Scanning; Chromatography, High Pressure Liquid; Electrophoresis, Polyacrylamide Gel; Food industries; Fruit and vegetable industries; Fundamental and applied biological sciences. Psychology; Gels - chemistry; Genotype; Globulins - analysis; Glycine max - chemistry; Glycine max - genetics; Hydrophobic and Hydrophilic Interactions; Rheology; Seed Storage Proteins; Soybean Proteins - chemistry
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/jf0105081

The β-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. Keywords: glycinin, β-conglycinin, soybean genotypes, protein characterization