Heating proteins and reducing sugars together reduces the solubility of the proteins. This can be seen as gel formation and the inability of the gel fragments or powders to go into solution in solvents that contain agents that should break disulfide bonds and non covalent associations. It would appear that the proteins become covalently linked one to another in an organized manner in dilute solutions. The creation of crosslinks could explain many of the characteristics of the sugar-protein gels, such as their high breakstrengths and clarity. Under conditions of high temperature and pressure that occur within the barrel of an extruder, protein crosslinking occurs if a reducing sugar is present. In extreme conditions, the reaction prevents a textured product being formed. Control of the induced crosslinking could enable better control of processes used extensively by food manufacturers.