Structural evolution, digestibility and inhibition on starch digestion of rice glutelin fibril aggregates as affected by incubation

Huang, Hui; Liu, Caiyi; Ma, Xiayin; Wu, Jinhong; Wang, Faxiang; Liu, Yongle; Li, Xianghong

doi:10.1016/j.ijbiomac.2022.06.140

Cited by 13 publications

(5 citation statements)

References 31 publications

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“…The peaks of thermal absorption and enthalpy changes (Δ H ) of SPI and SAFs are recorded in Table . All of the DSC thermograms presented endothermic peaks in the temperature range 38.5–65.1 and 140.4–169.6 °C, respectively, which may be attributed to the heat-induced disassembly of protein particles, amyloid fibrils, and their aggregates. ,, The varying temperatures at which the samples thermally decomposed indicated different structures in the fibrils that are produced and linked to concentration-regulated protein aggregation. ,, Relative to USPIs-2C, HSAFs-2C had lower thermal transition temperatures ( T o , T p , and T e ), suggesting that the developed SAFs at 2% became more heat-sensitive. When the PC was increased from 2 to 8%, the T p and Δ H (Peak II ) values of the resulting SAFs increased significantly ( P < 0.05).…”

Section: Resultsmentioning

confidence: 94%

“…This thermal response may be ascribed to the dissimilarities in their mesoscopic traits, as evidenced by distinct persistence lengths and height profiles. Consistent results were drawn in the work of Huang et al, who found that rigid fibrils and their aggregates required greater heat energy to disassemble the stable structures compared with other incubation times for fibrils.…”

Section: Resultsmentioning

confidence: 99%

“…amyloid fibrils, and their aggregates. 25,32,33 The varying temperatures at which the samples thermally decomposed indicated different structures in the fibrils that are produced and linked to concentration-regulated protein aggregation. 11,25,33 Relative to USPIs-2C, HSAFs-2C had lower thermal transition temperatures (T o , T p , and T e ), suggesting that the developed SAFs at 2% became more heat-sensitive.…”

Section: Analysis Of Saf Structure By Xrdmentioning

confidence: 99%

“…It can be deduced that larger fibril aggregates formed at higher PCs may prevent the ThT molecules from specifically binding to the β-sheet structures of the fibril backbone, albeit the dye ThT is highly sensitive. A similar case was also reported in the study undertaken by Huang et al, 25 who found that a reduction in the fluorescence intensity of protofibrils occurred due to the generation of hydrogen-bonded fibril aggregates upon prolonged incubation time.…”

Section: Analysis Of Fibril Conversion and Tht Fluorescence Intensitymentioning

confidence: 99%

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Concentration-Regulated Fibrillation of Soy Protein: Structure and In Vitro Digestion

Zheng

Gao

Chang

et al. 2023

J. Agric. Food Chem.

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The impact of protein types, heating temperatures, and times on protein fibrillation has been widely studied. However, there is little understanding of the influence of protein concentration (PC) on the protein fibril assembly. In this work, the structure and in vitro digestibility of soy protein amyloid fibrils (SAFs) were investigated at pH 2.0 and different PCs. Significant increases in fibril conversion rate and parallel β-sheets proportion were observed in SAFs upon increasing the PC from 2 to 8% (w/ v). The AFM images showed that curly fibrils were prone to form at 2−6% PCs, while rigid, straight fibrils developed at higher PCs (≥8%). As evidenced in XRD results, increasing PC led to a more stable structure of SAFs with enhanced thermal stability and lower digestibility. Moreover, positive correlations among PC, β-sheet content, persistence length, enthalpy, and total hydrolysis were established. These findings would provide valuable insights into concentration-regulated protein fibrillation.

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Section: Resultsmentioning

confidence: 94%

Section: Resultsmentioning

confidence: 99%

Section: Analysis Of Saf Structure By Xrdmentioning

confidence: 99%

Section: Analysis Of Fibril Conversion and Tht Fluorescence Intensitymentioning

confidence: 99%

See 2 more Smart Citations

Concentration-Regulated Fibrillation of Soy Protein: Structure and In Vitro Digestion

Zheng

Gao

Chang

et al. 2023

J. Agric. Food Chem.

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“…While rice starch offers advantages such as fine granules, non-allergenic properties, and strong acid resistance, it does have limitations. These include easy digestion, rapid absorption, and a high glycemic index (GI), which poses a significant risk to individuals with chronic conditions like diabetes and obesity [2].…”

Section: Introductionmentioning

confidence: 99%

A Study on the Structural and Digestive Properties of Rice Starch–Hydrocolloid Complexes Treated with Heat–Moisture Treatment

Zhang,

Dou,

Jia

et al. 2023

Foods

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Rice starch-hydrophilic colloid complexes (SHCs) were prepared by incorporating xanthan gum and locust bean gum into natural rice starch. Subsequently, they underwent hygrothermal treatment (H-SHC) to investigate their structural and digestive properties with varying colloid types and added amounts of H-SHC. The results demonstrated that heat–moisture treatment (HMT) led to an increase in resistant starch (RS) content in rice starch. This effect was more pronounced after the addition of hydrophilic colloid, causing RS content to surge from 8.42 ± 0.39% to 38.36 ± 3.69%. Notably, the addition of locust bean gum had a more significant impact on enhancing RS content, and the RS content increased with the addition of hydrophilic colloids. Enzyme digestion curves indicated that H-SHC displayed a lower equilibrium concentration (C∞), hydrolysis index (HI), and gluconeogenesis index (eGI). Simultaneously, HMT reduced the solubility and swelling power of starch. However, the addition of hydrophilic colloid led to an increase in the solubility and swelling power of the samples. Scanning electron microscopy revealed that hydrophilic colloid encapsulated the starch granules, affording them protection. X-ray diffraction (XRD) showed that HMT resulted in the decreased crystallinity of the starch granules, a trend mitigated by the addition of hydrophilic colloid. Infrared (IR) results demonstrated no formation of new covalent bonds but indicated increased short-range ordering in H-SHC. Rapid viscosity analysis and differential scanning calorimetry indicated that HMT substantially decreased peak viscosity and starch breakdown, while it significantly delayed the onset, peak, and conclusion temperatures. This effect was further amplified by the addition of colloids. Rheological results indicated that H-SHC displayed lower values for G′, G″, and static rheological parameters compared to natural starch. In summary, this study offers valuable insights into the development of healthy, low-GI functional foods.

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Effect of Different Valence Metal Ions on Rice Protein Fibrillation: Binding Mechanism, Structural Characterization and Rheology

Song

Zhang

et al. 2023

Food Biophysics

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Structural evolution, digestibility and inhibition on starch digestion of rice glutelin fibril aggregates as affected by incubation

Cited by 13 publications

References 31 publications

Concentration-Regulated Fibrillation of Soy Protein: Structure and In Vitro Digestion

Concentration-Regulated Fibrillation of Soy Protein: Structure and In Vitro Digestion

A Study on the Structural and Digestive Properties of Rice Starch–Hydrocolloid Complexes Treated with Heat–Moisture Treatment

Effect of Different Valence Metal Ions on Rice Protein Fibrillation: Binding Mechanism, Structural Characterization and Rheology

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