The effect of the N-linked glycans on structural features and physicochemical functions of soybean β-conglycinin homotrimers

β-Conglycinin is a trimeric protein consisting of three subunits, α,α′,and β, which are N-glycosylated. The α and α′ subunits contain extension regions in addition to core regions common to all subunits. We purified homogeneous trimers consisting of only α, α′, or β from mutant soybean cultivars containing β-conglycinin lacking one or two subunits: α homotrimers from an α′-lacking mutant, α′ homotrimers from an α-lacking mutant, and β homotrimers from an α-and α′-lacking mutant. Structural features and physicochemical functions of the three homotrimers were examined and compared with those of recombinant homotrimers having no N-linked glycans. The native homotrimers have secondary structures very similar to those of the recombinant ones. In analogy with the recombinant homotrimers, the native ones exhibit different thermal stabilities from one another (β>α′>α), and the native α and α′ homotrimers exhibit better solubility, emulsifying ability, and heat-induced association than the native β homotrimer. Further, the N-linked glycans contribute to solubilities of the three subunits at low ionic strength (μ=0.08) and to the emulsifying ability of the native β homotrimer. N-Linked glycans also prevent heat-induced associations of the native α and α′ homotrimers but do not contribute to the secondary structure and the thermal stability of β-conglycinin.