Enhancing the formation rate and level of oat globulin fibrils by microwave heating: Elucidation of potential mechanisms DOI
Mengdi Cai, Hongwei Cao, Sen Li

et al.

Food Hydrocolloids, Journal Year: 2025, Volume and Issue: unknown, P. 111327 - 111327

Published: March 1, 2025

Language: Английский

Study on the formation mechanism of pea protein nanofibrils and the changes of structural properties of fibril under different pH and temperature DOI
Chaoran Liu, Di Wu, Pengjie Wang

et al.

Food Hydrocolloids, Journal Year: 2024, Volume and Issue: 150, P. 109735 - 109735

Published: Jan. 4, 2024

Language: Английский

Citations

20
Study on the enhanced 3D printing performance of high internal phase emulsions using protein fibrosis strategy DOI
Ying Wang, Fengxian Guo,

H.C. Li

et al.

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: 297, P. 139975 - 139975

Published: Jan. 16, 2025

Language: Английский

Citations

2
Food-derived protein amyloid-like fibrils: Fibrillation mechanism, structure, and recent advances for the stabilization of emulsions DOI
Yue Xu, Chunmin Ma, Yang Yang

et al.

Food Hydrocolloids, Journal Year: 2023, Volume and Issue: 145, P. 109146 - 109146

Published: Aug. 4, 2023

Language: Английский

Citations

31
Production and characterization of amaranth amyloid fibrils from food protein waste DOI Creative Commons
Svitlana Mykolenko, Wei Long Soon, Raffaele Mezzenga

et al.

Food Hydrocolloids, Journal Year: 2023, Volume and Issue: 149, P. 109604 - 109604

Published: Dec. 2, 2023

Plant proteins self-assembly into amyloid fibrils is a promising modification to be introduced in emerging food and materials applications. Although the valorization of protein-rich side streams amaranth oil production completely missing, we show that double salt extraction provides recovery globulin fraction seed from waste with high purity complete protein solubility at acidic pH. We demonstrate silico propensity density amyloidogenic regions 11S storage Amaranthus hypochondriacus. further recovered can self-assemble under heat-induced hydrolysis. The nature was studied by thiazole orange (TO) fluorescence, SDS-PAGE, FTIR, CD, TEM, AFM. systematically investigated how temperature fibrillization affected unfolding, peptide release, as well its effect on tuning formation, growth, polymorphism fibrils. β-sheet-rich structured extracted exhibited mesoscopic rigid manifestation left-handed ribbons varying polymorphism. favourable conditions for extensive hydrolysis promote growth well-ordered thick twisted small-pitch extraordinary rigidity interpret these finding based structural models These results provide additional insight formation plant functional foods biocompatible materials, introduce pathway convert nanofibrils.

Language: Английский

Citations

26
Investigating the fibrillation behavior of Spirulina platensis protein: Self-assembly process and effects on emulsion stability DOI
Junwen Wang,

Wenchen Yu,

Jiayu Wang

et al.

Food Chemistry, Journal Year: 2025, Volume and Issue: 476, P. 143332 - 143332

Published: Feb. 10, 2025

Language: Английский

Citations

1
Amyloid fibrils from black kidney bean protein self-assemble into hydrogels: Impact of heating time on gel structure and rheological properties DOI
Shurui Wang, P. Liu,

Yiyu Zang

et al.

Food Chemistry, Journal Year: 2025, Volume and Issue: 476, P. 143406 - 143406

Published: Feb. 13, 2025

Language: Английский

Citations

1
The complex of arachin amyloid-like fibrils formed with ultrasound treatment and chitosan: A potential vehicle for betanin and curcumin with improved chemical stability and slow release in vitro DOI
Yang Qin, Xiaohong Yu, Jingwen Zhang

et al.

Food Hydrocolloids, Journal Year: 2025, Volume and Issue: unknown, P. 111272 - 111272

Published: Feb. 1, 2025

Language: Английский

Citations

1
Formation and structural characteristics of pea globulin amyloid-like fibrils pretreated with low-frequency magnetic field DOI
Qingqing Liu, Yang Qin, Yaru Wang

et al.

Food Hydrocolloids, Journal Year: 2023, Volume and Issue: 147, P. 109331 - 109331

Published: Sept. 23, 2023

Language: Английский

Citations

21
Exploring the self-assembly journey of oat globulin fibrils: From structural evolution to modified functionality DOI
Jinzhao Xu,

Mengqi Tang,

Danping Wang

et al.

Food Hydrocolloids, Journal Year: 2023, Volume and Issue: 149, P. 109587 - 109587

Published: Nov. 23, 2023

Language: Английский

Citations

19
Amyloid-like Aggregation of Wheat Gluten and Its Components during Cooking: Mechanisms and Structural Characterization DOI
Ying Liang, Hao Liu,

Yangyi Jie

et al.

Journal of Agricultural and Food Chemistry, Journal Year: 2024, Volume and Issue: 72(19), P. 11080 - 11093

Published: May 1, 2024

Amyloid-like aggregation widely occurs during the processing and production of natural proteins, with evidence indicating its presence following thermal wheat gluten. However, significant gaps remain in understanding underlying fibrillation mechanisms structural polymorphisms. In this study, amyloid-like behavior gluten components (glutenin gliadin) cooking was systematically analyzed through physicochemical assessment characterization. The fibrils (AFs) confirmed using X-ray diffraction Congo red staining, while Thioflavin T fluorescence revealed different patterns rates AFs growth among gluten, glutenin, gliadin. gliadin exhibited linear curves, those glutenin showed S-shaped shortest lag phase fastest rate (t1/2 = 2.11 min) observed glutenin. Molecular weight analyses primarily 10–15 kDa range, shifting to higher weights over time. Glutenin-derived had smallest ζ-potential value (−19.5 mV) most size increase post (approximately 400 nm). involve interchain reorganization, hydrophobic interactions, conformational transitions, leading additional cross β-sheets. Atomic force microscopy depicted varying fibril structures cooking, notably longer, taller, stiffer from

Language: Английский

Citations

7