Glutenin and dough tenacity

Assuming a random distribution of Cys residues within a glutenin polypeptide chain it has been calculated that about one sixth of an average chain (allowing for an intra‐chain SS loop) would be available for unfolding under stress. It is postulated that, because the unfolding of chains under stress has a magnifying effect on the effective molecular length of glutenin, a comparatively small range in the average number of chains per molecule (DP) is sufficient to encompass the levels of dough tenacities encountered in practice. Since the DP depends inversely on the concentration of Theologically active SH groups, according to the linear glutenin hypothesis, an explanation is provided for the great sensitivity of doughs to reducing agents and improvers, and for the indifferent correlation of dough properties with flour SH content.