SC+DoughBread+conditioners

From Dough and bread Conditioners:

Q & A :

1. How is the gluten development? The major proteins of bread, gliadin and glutenin, can be viewed as coiled or folded chains, with the structure stabilized by bonds between sulfur atoms (disulfide bonds) on adjacent areas of the molecules (intramolecular bonds). Mixing stretches the molecules and breaks the relatively weak bonds. During resting, the disulfide bonds can re-form either within (as before) or between molecules (intermolecular). When bonds form between molecules, the resulting structure (gluten) is much stronger than the individual proteins.

2. How reducing agents affect the gluten?Give example. They disrupt the disulfide bonds between and within protein molecules, weakening the protein structures. Since the intramolecular disulfide bonds are rapidly "disconnected," the proteins unfold quickly with less mixing. This can also soften the gluten where desired, as in biscuit dough, or can be used in conjunction with a slow-acting oxidizer to reduce mixing time. The most commonly used reducing agent, L-cysteine, works very quickly. Other reducers include sulfites, which can cause allergic reactions, and reduced glutathione in the form of deactivated yeast.