Dynamic Changes in Glutenin Macropolymer during Different Dough Mixing and Resting Processes

Abstract

The glutenin macropolymer (GMP), which is an important component of the glutenin protein in wheat flour, plays a prominent role in governing dough properties and breadmaking quality. This study investigated the changes in GMP properties during the mixing and resting stages of dough processing. The results show that the GMP content decreases by about 20.20% when the mixing time increases from 3 to 5 min, while increasing the resting time can lead to restoration of some GMP contents. Resting promotes greater formation of large-sized GMP particles, which is likely related to the increased disulfide bond content in the GMP during this process. In contrast, the mechanical force of mixing causes GMP depolymerization and formation of smaller particles. Furthermore, after mixing, the protein secondary structure tends to be disordered, the protein morphology becomes irregular, and the protein subunit ratio changes. Thus, mixing has many of the opposite effects to resting, although resting can (to some extent) restore the properties of the GMP after mixing. However, excessive resting time can lead to negative results, reflected in lower disulfide bond (SS) and GMP contents, and more irregular particle sizes. The presented results suggest that dough mixing induces rearrangement of the dough’s protein structure, and resting somewhat restores the chemical bonds and internal protein structure.