Cooking mediated wheat gluten aggregation behavior: Physicochemical properties and component changes

Líu, Hao; Zhang, Shengyang; Yan, Xuefeng; Wang, Jiayi; Liu, Mei; He, Bo; Zhang, Xia; Wang, Jinshui

doi:10.1016/j.foodhyd.2023.108957

Cited by 3 publications

(8 citation statements)

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“…Hydrophobic interactions play a crucial role in the recombination of wheat gluten. 22 Similarly, Zhu et al 53 demonstrated their equally significant role in fibril formation. To evaluate the impact of cooking on exposure of hydrophobic regions in AFs formed from various proteins, this study employed a widely used fluorescent hydrophobic probe, ANS.…”

Section: Average Size and ζ Potential Measurementsmentioning

confidence: 95%

“…Notably, the intensity of the spectrum in gliadin (Figure 1c) remained relatively unchanged upon heating, potentially attributed to the high thermal stability of gliadin. 22 These findings suggest that wheat gluten, glutenin, and gliadin all possess a core conducive to fibrillation. However, the intricate structural domains of these proteins and their poor solubility in aqueous solutions may present obstacles to the formation and detection of AFs in wheat gluten.…”

Section: Fourier Transform Infrared (Ft-ir) Spectroscopymentioning

confidence: 96%

“…This suggests that protein unfolding occurs at the beginning of cooking, exposing internal charged groups. 22 The fibrillation process, in turn, involves the reorganization of proteins, and continued cooking intensifies the degree of interstacking between proteins, thereby reducing the surface charge. The AFs glutenin and AFs gliadin exhibited a similar trend.…”

Section: Average Size and ζ Potential Measurementsmentioning

confidence: 99%

“…This blend exhibits diverse functional properties; gliadin, rich in aliphatic amino acids, contributes high surface hydrophobic peptides, imparting viscosity to the system. 22 On the other hand, glutenin, known for its abundant α-helix structure and high molecular weight, imparts elasticity to the system. The distinct amino acid compositions and arrangements within gliadin and glutenin lead to differential behaviors during the fibrillation process, 4 a phenomenon that has not been specifically addressed in existing studies.…”

Section: Introductionmentioning

confidence: 99%

“…Wheat gluten is a protein mixture comprising 40–50% gliadin and 30–40% glutenin. This blend exhibits diverse functional properties; gliadin, rich in aliphatic amino acids, contributes high surface hydrophobic peptides, imparting viscosity to the system . On the other hand, glutenin, known for its abundant α-helix structure and high molecular weight, imparts elasticity to the system.…”

Section: Introductionmentioning

confidence: 99%

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Amyloid-like Aggregation of Wheat Gluten and Its Components during Cooking: Mechanisms and Structural Characterization

Liang,

Liu,

Jie

et al. 2024

J. Agric. Food Chem.

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Amyloid-like aggregation widely occurs during the processing and production of natural proteins, with evidence indicating its presence following the thermal processing of wheat gluten. However, significant gaps remain in understanding the underlying fibrillation mechanisms and structural polymorphisms. In this study, the amyloid-like aggregation behavior of wheat gluten and its components (glutenin and gliadin) during cooking was systematically analyzed through physicochemical assessment and structural characterization. The presence of amyloid-like fibrils (AFs) was confirmed using X-ray diffraction and Congo red staining, while Thioflavin T fluorescence revealed different patterns and rates of AFs growth among wheat gluten, glutenin, and gliadin. AFs in gliadin exhibited linear growth curves, while those in gluten and glutenin showed S-shaped curves, with the shortest lag phase and fastest growth rate (t 1/2 = 2.11 min) observed in glutenin. Molecular weight analyses revealed AFs primarily in the 10− 15 kDa range, shifting to higher weights over time. Glutenin-derived AFs had the smallest ζ-potential value (−19.5 mV) and the most significant size increase post cooking (approximately 400 nm). AFs in gluten involve interchain reorganization, hydrophobic interactions, and conformational transitions, leading to additional cross β-sheets. Atomic force microscopy depicted varying fibril structures during cooking, notably longer, taller, and stiffer AFs from glutenin.

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Section: Average Size and ζ Potential Measurementsmentioning

confidence: 95%

Section: Fourier Transform Infrared (Ft-ir) Spectroscopymentioning

confidence: 96%

Section: Average Size and ζ Potential Measurementsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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