Superoxide involvement in the reduction of disulfide bonds of wheat gel proteins

The sodium dodecyl sulfate (SDS) insoluble gel proteins of wheat flour are converted under the influence of mixing energy and air or oxygen into SDS soluble proteins, which during the resting period after mixing reassociate into SDS insoluble gel proteins. These processes take place via cleavage and formation of disulfide (SS) bonds, respectively. During dough-mixing, O 2 is reduced to the superoxide anion ( O 2 −• ); its electron is transferred via an Mn, Cu-protein system to an SS bond, which is then reduced to SH groups. An Mn 3+-protein compound is responsible for the formation of new SS bonds.