Effect of Thermal Treatment on the Self-Assembly of Wheat Gluten Polypeptide

Abstract

Self-assembled fibrillation of wheat gluten is a common phenomenon in the daily production and processing of wheat flour products. The driving forces for its formation and the factors that influence the morphology of fibrils have not been thoroughly investigated. In this study, the effect of three bonding changes (breaking hydrogen bonds, strengthening hydrophobic interactions, and SH-SS exchange reactions) on gluten polypeptide (GP) fibrillation was simulated by adjusting the heating temperature (room temperature (RT), 45 °C, 65 °C, and 95 °C). The results showed that the breakage of hydrogen bonds could induce conformational transitions in GPs and help to excite fibrillation in GPs. Strengthened hydrophobic interactions significantly contributed to the fibrillation of GPs. Covalent crosslinks generated by SH-SS exchange reactions might also promote the fibrillation of GPs. GPs with different degrees of hydrolysis (4.0%, 6.0%, and 10.0%, represented by DH 4, DH 6, and DH 10, respectively) presented different extents of fibrillation, with DH 10 GPs having a higher propensity to fibrillation than DH 4 and DH 6 GPs. The results of Fourier’s transform infrared spectroscopy indicated that hydrophobic interactions drive the transition from a random coil and α-helix to a β-sheet. In addition, hydrophobic interactions also drive the intermolecular polymerization of GPs, resulting in larger molecular weight aggregates. The morphology presented by transmission electron microscopy showed that the greater the DH, the stronger the tendency for the worm-like aggregation of GPs.

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

“…The results indicated a gradual increase in the proportion of aggregates and β-sheet structures, accompanied by a decrease in the proportion of α-helix and random oil structures in the thermally induced formation of AFs gluten . Aggregation signifies a high density of β-sheet, serving as the predominant structure in AFs . Consistent with these findings, Bruun et al observed that cooking wheat gluten or treating it with transglutaminase led to a transition in protein structure from α-helix to β-sheet.…”

“…Aggregation signifies a high density of β-sheet, serving as the predominant structure in AFs. 49 Consistent with these findings, Bruun et al 50 observed that cooking wheat gluten or treating it with transglutaminase led to a transition in protein structure from α-helix to β-sheet. The three β-strand-rich structures in AFs glutenin before and after cooking exhibited increases of 2.50, 4.11, and 3.42% in aggregation, β-sheet, and antiparallel β-sheet, respectively.…”

High and ultra‐high temperature drying of fermented dried noodles: effect on noodle quality and starch properties

“…However, CLSM analysis of the gluten network structure at the periphery of the pores revealed that the UT treatment led to a more prominent aggregation of the gluten network and significantly higher ( P < 0.05 ) gluten network junction point than the CMT treatment (Table S1). Increasing drying temperature led to the denaturation and aggregation of higher levels of gluten into larger polymeric proteins, resulting in a more compact and continuous gluten network structure stabilised by hydrogen and disulphide bonds (Liu et al ., 2023). In contrast, the larger pores in the cross section of the UT samples than the CMT samples might be attributed to the UT‐mediated increase in the aggregation of the gluten network.…”

Comprehensive advances in the synthesis, fluorescence mechanism and multifunctional applications of red-emitting carbon nanomaterials

“…As a result, it contributes to narrowing the optical band gap of FCNMs, followed by the emission in the far red or near IR region with high uorescence quantum yield. [69][70][71][72][73][74] Other atoms like selenium, boron, and uorine are also utilized for shiing the wavelength to the red region aer doping at edges on the surface of the organic precursor. The band gap is opened by the incorporation of these heavy atoms into the carbon core.…”