Assessment of the protein quality of fourteen soybean [Glycine max (L.) Merr.] cultivars using amino acid analysis and two-dimensional electrophoresis

The protein quality of commercial soybeans varieties can be determined from their total protein content, their amino acid composition and from the ratio of glycinin to β-conglycinin, the major seed storage protein components. In this study 14 commercial soybean cultivars were assessed. There were significant differences in storage protein composition (P < 0.05) and in their valine, proline and phenylalanine contents (P < 0.01 to P < 0.001). Mean protein values among these varieties ranged from 29.8% to 36.1%. The total amino acid nitrogen (AAN) ranged from 89.6 to 95.1 g AA/16 g of nitrogen, corresponding to nitrogen values from 16.5 to 17.9 g AAN/100 g protein. All varieties contained a good balance of essential amino acids (EAA9), limited only in methionine. Two-dimensional gel electrophoretic (2-DE) separations, led to the establishment of high-resolution proteome reference maps, enabling polypeptide chain identification and calculation of the ratio of the constituent glycinin and β-conglycinin storage proteins of soybean. This method enables the assessment of the genetic variability of the soybean cultivars, which can then be correlated with their protein quality and food processing properties. These three methods can be used as very effective tools for assisting plant breeders in their selection of high quality soybean varieties.