Work

Changes in the rheology and aggregation behavior of wheat glutenin and gliadin mediated by low-sodium salt

Year: 2025

Type: article

Abstract: Reducing sodium in cereal-based foods without reducing quality is still a major challenge, largely because the mechanistic role of salt substitutes in modulating key gluten components is unclear. This study aimed to decipher the distinct responses of glutenin (Glu) and gliadin (Gli) to low-sodium salt (LSS). By analysis, we demonstrated that LSS improved elasticity, tensile resistance and strain-hardening ability of Glu. Size-exclusion chromatography and fluorescence spectroscopy revealed that aggregation and hydrophobic exposure were promoted in Glu. Atomic force microscopy visualized the formation of larger Glu aggregates, while LF- 1 H NMR indicated a more tightly hydrated protein network. In contrast, Gli exhibited weaker structural and functional changes. In short, the efficacy of LSS was not uniform but structurally selective: it primarily targeted and reinforced Glu network due to Glu's unique polymeric structure, which was highly sensitive to ionic environment. This work provided mechanistic foundation for the rational design of sodium-reduced cereal products. • Mechanistic analysis of low-sodium salt action on isolated gluten components. • Glutenin's polymeric structure dictated its superior responsiveness to Na + /K + . • Proposed a structure-dependent principle for rational salt reduction design. • Integrates rheology, spectroscopy, and microscopy to span macro-to-nano scales.

Source: Food Chemistry X

DOI: 10.1016/j.fochx.2025.103439

Authors: Xiaohua Wang, Jinshui Wang, Xia Zhang, Ying Liang, Zhen Li, Zhilu Ai

Institutions: Henan Agricultural University, Henan University of Technology

Language: English

Topic: Proteins in Food Systems

Subfield: Food Science

Field: Agricultural and Biological Sciences

Domain: Life Sciences

SDG: Zero hunger

Open Access status: gold

Estimated APC paid: $2,330