Changes  In Gluten Proteins During Dough Formation

Initially, gluten is formed when flour and water are mixed together. The proteins in the flour, glutenin and gliadin cross  link, using water as a vehicle to form gluten. Enhancing this gluten structure  is important relative to developing a gas retaining structure in the chapati/bread.   When the hydrated bread flour is mixed and kneaded, the gluten proteins orient themselves aligns and partially unfolded. This enhances hydrophobic interaction and formation of disulphide bridges through -S-S- interchange reactions.  A  3-dimensional viscoelastic protein network is established, as the initial gluten particles transform into this membrane (film), thus serving to entrap starch  granules and other flour components.  Cleavage  of disulphide bridges by reducing agents such as cysteine,  destroys the cohesive structure of hydrated gluten and  bread dough ;  the addition of  agents  such  as  bromates,  increase  toughness    and elasticity. "Strong" flours from certain wheat varieties require long mixing time and give very cohesive dough. "Weak flours"  are less effective and  gluten network breaks down when the energy  or duration of mixing exceeds a certain level, probably because of -S-S-  bonds  are ruptured (especially in absence of  air). 

Dough strength  appears  to  be  related to a  large   content  of  high molecular   weight glutenins including totally insoluble  "residue proteins". From experiments with "reconstituted" wheat flours  of varying  gliadin and glutenin  ratios, it can be  postulated  that the  glutenins are responsible for the  elasticity,  cohesiveness and  mixing  tolerance  of  dough  whereas  gliadins   facilitate fluidity,   extensibility  and  expansion  of  the  dough, thus contributing  to a larger bread loaf volume. A proper balance of the proteins is essential for bread making.  Excessive  cohesion (glutenins)  inhibit \the expansion of trapped CO2 bubbles  during fermentation,  the rise of the dough and the subsequent  presence of  open  air cells in the bread  crumb.  Excessive extensibility (gliadins) results in gluten films that are weak and permeable; thus retention of CO2 is poor and dough collapse may occur.