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

摘要

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