Mixing history affects gluten protein recovery, purity, and glutenin re-assembly capacity from optimally developed flour–water batters

Abstract

Batters, from three wheat cultivars, were mixed up to their maximal consistency ( t peak ) at different mixing speeds ( N) and flour/water ratios [Auger, F., Morel, M.H., Lefebvre, J., Dewilde, M., Redl, A., 2008. A parametric and microstructural study of the formation of gluten network in mixed flour–water batter. Journal of Cereal Science 48, 349–358]. Gluten and starch were extracted from those batters using a process which included two successive steps: dilution and sieving. In order to reveal the specific influence of the mixing step, a standardized gentle washing and sieving procedure was selected. Mixing the batters at t peak guaranteed a high and stable gluten protein recovery (ca. 82%) irrespective of mixing conditions. SE-HPLC analysis of protein, from flours and batters sampled at t peak , demonstrated that mixing led to the almost total breakdown of the unextractable glutenin polymers (ca. 80%), whereas their re-assembly occurred during gluten extraction. The extent of glutenin re-assembly in gluten was influenced by the batter mixing history and was mainly related to the number of mixing rotations ( N.t peak ). Gluten protein contents were also found related to N.t peak . We proposed that the leaching of starch from the batter during gluten extraction was controlled by the elasticity of the protein network, i.e. the gluten content in unextractable glutenin. An innovating scheme relating the glutenin re-assembly capacity to the irreversible thiol protein oxidation is proposed.