Genetic mapping and validation of the loci controlling 7S α' and 11S A-type storage protein subunits in soybean [Glycine max (L.) Merr.].

Four soybean storage protein subunit QTLs were mapped using bulked segregant analysis and an F population, which were validated with an F RIL population. The storage protein globulins β-conglycinin (7S subunit) and glycinin (11S subunits) can affect the quantity and quality of proteins found in soybean seeds and account for more than 70% of the total soybean protein. Manipulating the storage protein subunits to enhance soymeal nutrition and for desirable tofu manufacturing characteristics are two end-use quality goals in soybean breeding programs.

Molecular analysis of glycinin genes in soybean mutants for development of gene-specific markers.

Soybean mutant lines that differ in 11S glycinin and 7S β-conglycinin seed storage protein subunit compositions were developed. These proteins have significant influence on tofu quality. The molecular mechanisms underlying the mutant lines are unknown.

Protein recovery in soymilk and various soluble fractions as a function of genotype differences, changes during heating, and homogenization.

Harovinton, a variety of tofu type soybean, and 11 derived null soybean genotypes lacking specific glycinin (11S) and beta-conglycinin (7S) protein subunits were investigated to determine whether changes in protein composition affected the protein recovery in soymilk and its soluble fractions after various centrifugation steps. As both heating and homogenization have a marked effect on the increase in protein solubility, the changes occurring during these processing steps were studied for each soybean genotype. Harovinton and 11S-null genotypes showed significantly higher protein yields than the other genotypes evaluated.

Soybean seed lustre phenotype and surface protein cosegregate and map to linkage group E.

Soybean (Glycine max (L.) Merr.) seeds vary in their surface properties.