Effect of the Molecular Interactions between β-lactoglobulin and Gliadin on the Baking Quality

Abstract

　In this study, the gliadin that is water-solublized by the action of β-Lg was identified. As a result, it became clear that β-Lg specifically interacts with the most hydrophilic ω-gliadin in each gliadin (α, β, γ, ω), and the ω-gliadin is desorbed from gliadin aggregates and becomes water-soluble. In contrast, regarding the recovery factors of baking quality using heated skim milk, where β-Lg forms a heated complex with κ-CN, the specificity of ω-gliadin is negated due to κ-CN's high affinity to each gliadin; thus, desorption from gliadin aggregates is inhibited. Furthermore, when gliadin which ω-gliadin was removed, was added to wheat flour dough, the formation of the dough becomes poor and gas retention of the dough reduced. It became clear that the degradation of the bread with skim milk is caused where ω-gliadin is desorbed from the gliadin aggregates due to the action of β-Lg.