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Wheat gluten proteins serve as the largest protein molecules in nature and play key roles in breadmaking quality formation. In this study, we used a pair of Glu-A1 allelic variation lines to perform a comprehensive investigation on the effects of Glu-A1a encoded 1Ax1 subunit on gluten physicochemical properties, molecular structures and breadmaking quality. The results showed that the presence of the 1Ax1 subunit significantly increased gluten content, leading to marked improvement of dough rheological properties. Meanwhile, gluten physicochemical properties such as foaming ability and foaming stability, oil/water-holding capacity, emulsifying activity, disulfide bond content, and gluten degradation temperature were significantly improved. A confocal laser scanning microscope analysis revealed that the 1Ax1 subunit drastically enhanced gluten microstructure. Gluten secondary structure analysis by Fourier transform infrared spectroscopy and laser scanning microscope-Raman spectroscopy indicated that 1Ax1 subunit significantly promoted β-turn and β-sheet content and reduced α-helix content. Three-dimensional structure analysis by AlphaFold2 revealed a similar structural feature of 1Ax1 with the superior quality subunit 1Ax2*. Correlation and principal component analyses demonstrated that α-helix and β-sheet content had a significant correlation with dough rheological properties, gluten physicochemical properties and breadmaking quality. Our results showed that 1Ax1 subunit positively affected gluten molecular structure and quality formation. • 1Ax1 improved dough rheological properties and gluten physicochemical properties. • Connectivity and uniformity of gluten microstructure were enhanced by 1Ax1 subunit. • The 1Ax1 subunit promoted gluten disulfide bond content and foaming properties. • Loaf volume and inner structures were positively affected by the 1Ax1 subunit. • α-Helix and β-sheet were the key predictors for gluten strength and breadmaking quality. [ABSTRACT FROM AUTHOR]

This study evaluated the effects of starch with varying degree of debranching on the rheological, thermal, and structural properties of heat-induced gluten gel. As the duration of starch debranching treatment increased from 0 to 8 h, the viscoelasticity of the gel containing debranched starch (DBS) improved. Compared with the gluten gel (G), the gel strength of the G + DBS (8 h) sample increased by 65.2 %. The degradation temperature of gluten was minimally affected by DBS, while the weight loss rate increased by 4.4 %. Furthermore, the α-helical structure of gluten decreased, concomitant with an increase in β-sheet content. Notably, DBS treated for 8 h exhibited more hydrogen bonds with the tyrosine of gluten and triggered disulfide bridge conformation to transition from g-g-g to t-g-g, thereby reducing the stability of the molecular conformation of gluten proteins, as evidenced by the decreased height and width of the molecular chains observed in atomic force microscopy images. Overall, the composite gel structure induced by DBS exhibited a more continuous and homogeneous owing to the improved compatibility between DBS and gluten proteins, favoring the formation of a robust gel. These findings provide valuable insights for utilizing DBS to enhance gluten gel properties. [Display omitted] • The strength of gluten gel was improved by debranched starch (DBS). • Highly DBS generated a microstructure compatible with gluten, and improved gel texture. • DBS decreased α-helical in gluten and destabilized S S bridges. • DBS hindered the cross-linking of gliadin or low molecular weight glutenin. • The aggregation of gluten molecular chains at the nanoscale was inhibited by DBS. [ABSTRACT FROM AUTHOR]

Herein, we investigated the effects of gluten proteins (Pr) on the structure, physicochemical properties, and in vitro digestibility of wheat starch-lauric acid (WS-LA) complexes under various cooking methods (steaming, boiling, and baking). There was no ternary complex formation between WS, LA, and Pr in the samples after different cooking methods. Scanning electron microscopy (SEM) and fluorescence microscopy showed variation in size, structure and distribution of WS-LA of WS-LA-Pr samples after cooking. An increase in the intensity of V-type diffraction peak and thermal stability was observed in steamed and baked samples, however, opposite trend was noticed in boiled sample. Additionally, a higher 1022/995 cm−1 absorbance ratio was noted in WS-LA-Pr sample treated with boiling than other cooking methods. Further, in vitro resistance to enzymatic hydrolysis was improved in samples treated with steaming and baking compared with boiled treated samples. In sum, this study may offer a thorough understanding on how these interactions take place during food processing, to optimize the production and development of new food products with desired microstructure and functionality features. [Display omitted] [ABSTRACT FROM AUTHOR]

Understanding the interplay between gluten and wheat starch is crucial for elucidating the digestibility mechanism of gluten in wheat-based products. However, this mechanism remains under-investigated. This study sought to elucidate the influence of starch-induced protein structural modifications on gluten digestion. Our findings revealed that starch considerably enhanced gluten digestion. In the presence of starch, gluten protein digestibility increased from 10.91 % (in the control group with a gluten-to-starch ratio of 1:0) to 14.40 % (in the complex with a gluten-to-corn starch ratio of 1:1). The diminished gluten protein digestibility due to starch may be ascribed to modifications in protein configuration and aggregation behavior. Morphological studies suggested that starch not only functioned as filler particles but also diluted the gluten matrix. A protein network assessment further affirmed that both the junction density and branching rate of gluten proteins decreased notably by 29.9 % and 25.1 %, respectively. Conversely, lacunarity increased by 1.92-fold, compromising the cohesiveness and connectivity of the gluten matrix. Elevated starch concentrations suppressed the formation of disulfide bonds, impeding gluten protein aggregation. Concurrently, gluten-starch interactions were governed by hydrogen bonds and hydrophobic associations. In summary, starch augmented gluten protein digestibility by curtailing their polymerization. This revelation might offer novel perspectives on optimizing gluten protein digestion and utilization. [Display omitted] • Starch facilitated gluten digestion by inhibiting its aggregation. • Starch changed the rheological and thermal properties of gluten proteins. • The network structure of gluten was weakened by starch. • Starch interfered with the formation of disulfide bonded gluten aggregates. [ABSTRACT FROM AUTHOR]