Recently, the Innovation Team of Cereal Processing and Quality Control at the Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences (IFST-CAAS), systematically reviewed the allelic variation and structural characteristics of wheat high-molecular-weight glutenin subunits (HMW-GSs), as well as the mechanisms by which they regulate dough strength and extensibility. The work was published in Comprehensive Reviews in Food Science and Food Safety, a leading international journal in food science (JCR Q1, IF = 15.6). Hongwei Zhou, a visiting PhD student of the 2023 cohort at IFST-CAAS, is the first author, while Associate Prof. Yingquan Zhang and Prof. Boli Guo are the co-corresponding authors.

Dough strength and extensibility directly determine the processing suitability of wheat flour and the quality of wheat-based products. The review summarizes findings from studies using natural wheat populations and near-isogenic lines and highlights the distinct contributions of HMW-GS allelic variation to dough rheological properties. At the molecular level, the structural basis underlying HMW-GS-mediated regulation of dough rheology is discussed hierarchically from primary sequence and secondary structure to tertiary conformation and protein network organization. On this basis, a multidimensional structure–function framework is proposed. Loop-chain motifs and helical structures impart molecular elasticity, while disulfide bonds crosslink HMW-GSs containing these elastic structural units into an integrated protein network. Non-covalent interactions, including hydrogen bonding, hydrophobic interactions, and ionic interactions, further contribute synergistically to network assembly and stabilization. Dough strength is primarily regulated by disulfide-bond crosslinking density and the stability of β-sheet chain-like structures, whereas extensibility is more closely associated with the deformability of β-turn loop regions and the flexibility of helical structures. Substitutions at key amino acid sites, including cysteine substitutions such as Cys10Ser-N, Cys40Ser-N, Ser8Cys-CRD, Tyr612Cys-CRD, and Cys25Ser-N, as well as non-cysteine substitutions such as Gly244Glu-CRD in the Ax1 subunit, can substantially alter dough strength and extensibility by modifying local conformations and intermolecular interactions.

The review further proposes that future research should strengthen interdisciplinary integration among breeding, food science, computational biology, synthetic biology, and artificial intelligence. Greater use of unique genetic resources, high-resolution characterization techniques, and molecular dynamics simulations will facilitate deeper understanding of HMW-GS structures and assembly mechanisms. Establishing predictive relationships linking sequence, structure, molecular interactions, and rheological quality will ultimately support the precise design and targeted regulation of gluten protein functionality.

This work was supported by the Special National Key Research and Development Plan, the Agricultural Science and Technology Innovation Program of the Chinese Academy of Agricultural Sciences, and other research programs.

Original article: http://dx.doi.org/10.1111/1541-4337.70585