Effect of the Molecular Interaction between Wheat Proteins and β-lactoglobulin on Wheat-flour Dough Formation

Abstract

　Here we investigated the effect of skim-milk proteins on both the decline in baking quality and on the reversal of the decline in baking quality of skim milk. β-lactoglobulin (β-Lg) molecule interacted with a part of gliadin and lysed the gliadin molecules. In case of the heated mixture of β-Lg and κ-casein (κ-CN), the influence of β-Lg on gliadin resolvability was low. Further, these results revealed that the decline in the baking quality of non-heated skim milk or low-heated skim milk was because of the dissolved part of gliadin. In addition, the results suggest that the decline in the baking quality of high-heated skim milk was reversed because of the influence of β-Lg on gliadin resolvability; hydrophobic interactions of the heated polymer of β-Lg and κ-CN with gliadin reduced the resolvability of gliadin.