Impact of heat and enzymatic treatment on ovalbumin amyloid-like fibril formation and enzyme-induced gelation

Huyst, Arne M.R.; Deleu, Lomme J.; Luyckx, Trui; Meeren, Louis Van der; Housmans, Joëlle A.J.; Grootaert, Charlotte; Monge-Morera, Margarita; Delcour, Jan A.; Skirtach, André G.; Rousseau, Frédéric; Schymkowitz, Joost; Dewettinck, Koen; Meeren, Paul Van der

doi:10.1016/j.foodhyd.2022.107784

Cited by 17 publications

(3 citation statements)

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“…Nevertheless, they are of great interest from the technological perspective. For example, food-derived protein fibrils, which are gaining interest from the food industry because of their superior technofunctional properties (including gelling and foaming), often adopt a curly fibril morphology. , …”

Section: Introductionmentioning

confidence: 99%

“…For example, food-derived protein fibrils, which are gaining interest from the food industry because of their superior technofunctional properties (including gelling and foaming), often adopt a curly fibril morphology. 26,27 Despite its apparent ubiquity, the curly fibril morphology has not yet been recognized as a separate fibril category, and a systematic nomenclature has been lacking in the literature. Indeed, the morphology we here call ″curly″ has been referred to by many names: (semi)flexible, 28,29 worm-like, 30,31 curvilinear, 25,32 curved, 15,33 proto, 16,34,35 and curly fibrils.…”

Section: ■ Introductionmentioning

confidence: 99%

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Investigating the Sequence Determinants of the Curling of Amyloid Fibrils Using Ovalbumin as a Case Study

et al. 2022

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Highly ordered, straight amyloid fibrils readily lend themselves to structure determination techniques and have therefore been extensively characterized. However, the less ordered curly fibrils remain relatively understudied, and the structural organization underlying their specific characteristics remains poorly understood. We found that the exemplary curly fibrilforming protein ovalbumin contains multiple aggregation prone regions (APRs) that form straight fibrils when isolated as peptides or when excised from the full-length protein through hydrolysis. In the context of the intact full-length protein, however, the regions separating the APRs facilitate curly fibril formation. In fact, a metaanalysis of previously reported curly fibril-forming proteins shows that their inter-APRs are significantly longer and more hydrophobic when compared to straight fibril-forming proteins, suggesting that they may cause strain in the amyloid state. Hence, inter-APRs driving curly fibril formation may not only apply to our model protein but rather constitute a more general mechanism.

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Section: Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

Investigating the Sequence Determinants of the Curling of Amyloid Fibrils Using Ovalbumin as a Case Study

et al. 2022

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“…In contrast, the ThT fluorescence intensity of the SAFs showed a downward trend as the PC rose (Figure b). This change is supported by the findings of Huyst et al that the ThT fluorescence intensity of amyloid fibrils was reduced when protein aggregation was promoted. 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.…”

Section: Resultsmentioning

confidence: 99%

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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Remodeling mechanism of gel network structure of soy protein isolate amyloid fibrils mediated by cellulose nanocrystals

Zhou,

Lv,

Wang

et al. 2024

Carbohydrate Polymers

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Impact of heat and enzymatic treatment on ovalbumin amyloid-like fibril formation and enzyme-induced gelation

Cited by 17 publications

References 100 publications

Investigating the Sequence Determinants of the Curling of Amyloid Fibrils Using Ovalbumin as a Case Study

Investigating the Sequence Determinants of the Curling of Amyloid Fibrils Using Ovalbumin as a Case Study

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

Remodeling mechanism of gel network structure of soy protein isolate amyloid fibrils mediated by cellulose nanocrystals

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