The high molecular weight glutenin subunit forms the skeleton by intermolecular disulfide bond， while the low molecular weight glutenin subunit binds to the skeleton by disulfide bond， and the aggregates are further formed by non-covalent interactions such as hydrophobic interaction， hydrogen bond and electrostatic interaction between the skeletons. Aggregates that are so complex that even sodium dodecyl sulfate solution cannot disperse or dissolve are called glutenin macropolymer. The aggregation and deaggregation of glutenin macropolymer has great influence on flour production， dough viscoelasticity and relative sensory quality. The article summarizes the variation in glutenin macropolymer content and aggregation behavior from wheat kernel to flour and dough processing. During wheat storage， the content of glutenin macropolymer increased， indicating that glutenin gradually accumulated. In the center of wheat， the proportion of glutenin macropolymer to total protein was higher， indicating that more protein aggregation occurred in grain center. When mixing flour and water to form dough， the glutenin particles absorb water and swell， and the glutenin macropolymer content gradually decreases， indicating that the aggregation degree decreases as well. During the resting process， glutenin macropolymer content increased， indicating glutenin reaggregation. The analysis of dynamic equilibrium of protein aggregation and deaggregation at different levels is helpful to reveal the mechanism of glutenin macropolymers changes in wheat dough processing， which has importance in modulating gluten formation and dough viscoelasticity.