Food and Fermentation Industries >

2026 , Vol. 52 >Issue 1: 277 - 283

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.042505

Structural characterization and functional characteristics of amyloid fibrotic aggregation of 11S protein in fava bean

  • CHEN Hui ,
  • ZHOU Mengyuan ,
  • XU Zhe ,
  • LIN Xuemei ,
  • ZHAO Wenzhong ,
  • XU Zhihao ,
  • DING Xiaoqi ,
  • DING Yuting
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  • 1(College of Food Science and Technology, Zhejiang University of Technology, Hangzhou 310014, China)
    2(College of Life Sciences, Key Laboratory of Biotechnology and Bioresources Utilization, Dalian Minzu University, Dalian 116600, China)
    3(Lafang Jiahua Co.Ltd., Shantou 515041, China)
    4(Food Science Research Institute of Zhangzhou, Zhangzhou 363000, China)

Received date: 2025-02-25

  Revised date: 2025-05-19

  Online published: 2026-01-22

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Abstract

Food-borne protein amyloid fibrotic aggregation has unique structural properties, and fava bean 11S protein (FP) shows great potential as a sustainable protein resource.This study investigated the dynamic evolution of amyloid fibrotic aggregation of 11S protein in fava bean (FPF) during its formation, including its structural characterization and functional characteristics.6 g/100 mL of FP was treated by acid heat treatment (pH 2, 85 ℃) for different time (0-24 h) to obtain FPF.The processed samples were characterized by Thioflavin T, fluorescence, dityrosine, transmission electron microscopy and fourier infrared spectroscopy.The results showed that FP was first hydrolyzed into polypeptide during acid heat, and then self-assembled into β-folded FPF (increased from 34.44% at 0 h to 45.89% at 24 h).The functional properties of FPF were characterized by foaming, emulsifying and gelling properties.Compared with FP, FPF had better foaming, emulsifying and gelling properties after 24 h reaction.In addition, FPF did not show cytotoxicity in vitro cell experiments.This study provides theoretical support for the formation of FPF.

Key words： fava bean protein; 11S protein; amyloid fibrotic aggregation; structural features; functional characteristics

Cite this article

CHEN Hui , ZHOU Mengyuan , XU Zhe , LIN Xuemei , ZHAO Wenzhong , XU Zhihao , DING Xiaoqi , DING Yuting . Structural characterization and functional characteristics of amyloid fibrotic aggregation of 11S protein in fava bean[J]. Food and Fermentation Industries, 2026 , 52(1) : 277 -283 . DOI: 10.13995/j.cnki.11-1802/ts.042505

References

[1] WANG Z M, LAN T T, JIANG J, et al.On the modification of plant proteins:Traditional methods and the hofmeister effect[J].Food Chemistry, 2024, 451:139530.
[2] 王悦, 管春花, 毕洪, 等.植物蛋白的降脂功效及其应用潜力[J].食品工业科技, 2025, 46(2):412-421.
WANG Y, GUAN C H, BI H, et al.Lipid-lowering efficacy of plant proteins and their application potential[J].Science and Technology of Food Industry, 2025, 46(2):412-421.
[3] JOHANSSON M, JOHANSSON D, STRÖM A, et al.Effect of starch and fibre on faba bean protein gel characteristics[J].Food Hydrocolloids, 2022, 131:107741.
[4] JOHANSSON M, KARKEHABADI S, JOHANSSON D P, et al.Gelation behaviour and gel properties of the 7S and 11S globulin protein fractions from faba bean (Vicia faba var.minor) at different NaCl concentrations[J].Food Hydrocolloids, 2023, 142:108789.
[5] GUEGUEN J, CERLETTI P.Proteins of Some Legume Seeds:Soybean, Pea, Fababean and Lupin[M].Boston, MA:Springer US, 1994.
[6] 王金梅, 王梦萍, 韦翠兰, 等.大豆球蛋白的纤维聚集体行为及其稳定性研究[J].现代食品科技, 2017, 33(11):42-48;118.
WANG J M, WANG M P, WEI C L, et al.Fibrillar aggregation behavior and stability of soy globulin[J].Modern Food Science and Technology, 2017, 33(11):42-48;118.
[7] 彭圆, 翟月滢, 刘采怡, 等.米谷蛋白淀粉样纤维聚集体自组装过程中蛋白质结构演变、功能性质及体外消化性研究[J].中国食品学报, 2023, 23(3):30-38.
PENG Y, ZHAI Y Y, LIU C Y, et al.Studies on the structural evolution, functional and in vitro digestive properties of rice glutelin during the self-assembly of the amyloid fibril aggregates[J].Journal of Chinese Institute of Food Science and Technology, 2023, 23(3):30-38.
[8] DONG W Y, ZHANG X Y, DING L X, et al.Enhancement of emulsification properties by modulation of egg white protein fibril structure with different heating times[J].Food Hydrocolloids, 2023, 135:108203.
[9] XU J Z, TANG M Q, WANG D P, et al.Exploring the self-assembly journey of oat globulin fibrils:From structural evolution to modified functionality[J].Food Hydrocolloids, 2024, 149:109587.
[10] HERNEKE A, LENDEL C, KARKEHABADI S, et al.Protein nanofibrils from fava bean and its major storage proteins:Formation and ability to generate and stabilise foams[J].Foods, 2023, 12(3):521.
[11] SUCHKOV V V, POPELLO I A, GRINBERG V Y, et al.Isolation and purification of 7S and 11S globulins from broad beans and peas[J].Journal of Agricultural and Food Chemistry, 1990, 38(1):92-95.
[12] KUTZLI I, ZHOU J T, LI T, et al.Formation and characterization of plant-based amyloid fibrils from hemp seed protein[J].Food Hydrocolloids, 2023, 137:108307.
[13] TANG C H, WANG C S.Formation and characterization of amyloid-like fibrils from soy β-conglycinin and glycinin[J].Journal of Agricultural and Food Chemistry, 2010, 58(20):11058-11066.
[14] LIU C R, WU D, WANG P J, et al.Study on the formation mechanism of pea protein nanofibrils and the changes of structural properties of fibril under different pH and temperature[J].Food Hydrocolloids, 2024, 150:109735.
[15] AROSIO P, KNOWLES T P J, LINSE S.On the lag phase in amyloid fibril formation[J].Physical Chemistry Chemical Physics, 2015, 17(12):7606-7618.
[16] MAINA M B, AL-HILALY Y K, OAKLEY S, et al.Dityrosine cross-links are present in Alzheimer’s disease-derived tau oligomers and paired helical filaments (PHF) which promotes the stability of the PHF-core tau (297-391) in vitro[J].Journal of Molecular Biology, 2022, 434(19):167785.
[17] LIU Z W, TANG P P, LIU C, et al.Promoting ovalbumin amyloid fibrils formation by cold plasma treatment and improving its emulsifying properties[J].Food Hydrocolloids, 2025, 158:110531.
[18] XU Z J, WANG X S, GAO Y, et al.Structural insights into acidic heating-induced amyloid fibrils derived from soy protein as a function of protein concentration[J].Food Hydrocolloids, 2023, 145:109085.
[19] JI F Y, XU J J, OUYANG Y Y, et al.Effects of NaCl concentration and temperature on fibrillation, structure, and functional properties of soy protein isolate fibril dispersions[J].LWT, 2021, 149:111862.
[20] ANDERSEN C B, YAGI H, MANNO M, et al.Branching in amyloid fibril growth[J].Biophysical Journal, 2009, 96(4):1529-1536.
[21] OLUWAJUYITAN T D, ALUKO R E.Structural and functional properties of fava bean legumin and vicilin protein fractions[J].International Journal of Food Science & Technology, 2024, 59(9):6698-6716.
[22] YI J, HE Q Y, PENG G F, et al.Improved water solubility, chemical stability, antioxidant and anticancer activity of resveratrol via nanoencapsulation with pea protein nanofibrils[J].Food Chemistry, 2022, 377:131942.
[23] WANG K X, ZHANG J, FU Z Y, et al.Oleogels based on peanut protein isolate fibrils:Structural characterization dependent on induction time and suitability in marguerite biscuits[J].Food Hydrocolloids, 2024, 154:110106.
[24] YU Z C, LI N, LIU Y A, et al.Formation, structure and functional characteristics of amyloid fibrils formed based on soy protein isolates[J].International Journal of Biological Macromolecules, 2024, 254:127956.
[25] CAO Z C, WANG X S, ZHAO J W, et al.Elucidating the modulatory influence of Hofmeister divalent ions on the structural dynamics and rheological properties of soy protein amyloid fibrils[J].Food Hydrocolloids, 2024, 151:109871.
[26] LI T, WANG L, GENG H, et al.Formation, structural characteristics, foaming and emulsifying properties of rice glutelin fibrils[J].Food Chemistry, 2021, 354:129554.
[27] WANG R, WANG L H, WEN Q H, et al.Combination of pulsed electric field and pH shifting improves the solubility, emulsifying, foaming of commercial soy protein isolate[J].Food Hydrocolloids, 2023, 134:108049.
[28] XU D, ZHOU J T, SOON W L, et al.Food amyloid fibrils are safe nutrition ingredients based on in-vitro and in-vivo assessment[J].Nature Communications, 2023, 14:6806.
[29] ZHOU F Z, ZHANG L P, ZHENG M X, et al.Effects of calcium sulfate on soy protein isolate-based emulsion microgels[J].LWT, 2024, 205:116562.
[30] 刘丽莉, 段京瑶, 郭悦, 等.明胶和马铃薯淀粉对大豆分离蛋白凝胶3D打印性能的影响[J].食品与发酵工业, 2025, 51(13):253-260.
LIU L L, DUAN J Y, GUO Y, et al.Effects of gelatin and potato starch on the 3D printing performance of soy protein isolate gels[J].Food and Fermentation Industries, 2025, 51(13):253-260.
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