The effects of reductants and oxidants on the functionality of gluten
proteins during dough mixing were studied for seven mixing parameters
using a prototype 2-g mixograph. Structural changes in the dough prote
ins were monitored by size-exclusion high-performance liquid chromatog
raphy and by multistacking sodium dodecyl sulfate polyacrylamide gel e
lectrophoresis. Using dithiothreitol as the reducing agent, experiment
al conditions were established that resulted in partial reduction of t
he glutenin polymers and radical changes in mixing parameters. Studies
of the effects of iodate, bromate, permanganate, and hydrogen peroxid
e on reduced doughs showed that careful selection of oxidant concentra
tion and oxidation conditions allowed an essentially complete recovery
of the original dough mixing properties. Size-exclusion high-performa
nce liquid chromatography and electrophoresis studies showed that samp
les reoxidized under optimum conditions had protein size distributions
almost identical to those of control samples. This test system provid
es a basis for directly evaluating hypotheses on the functional roles
of specific glutenin subunits by incorporating them into reduced dough
s by oxidation.