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Cited by 60Proteins in Food SystemsSupramolecular Self-Assembly in MaterialsProtein Structure and Dynamics

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Production and characterization of amaranth amyloid fibrils from food protein waste

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Mykolenko, Svitlana, Soon, Wei Long, Mezzenga, Raffaele·2024·Food Hydrocolloids
DOI 10.1016/j.foodhyd.2023.109604
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Abstract

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

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  • Further structuring routes can drive proteins toward distinct results, including compact particles in the nano-to submicron range or extended fibrillar/amyloid-like assemblies.

    “Further structuring routes can drive proteins toward distinct results, including compact particles in the nano-to submicron range or extended fibrillar/amyloid-like assemblies.”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Mykolenko et al., 2024

    Section 3.4.5 reports micrometre-long amyloid fibrils alongside spherical aggregates of 10–20 nm and globular particles of 40–80 nm. It also reports that higher incubation temperatures produced longer, more ordered fibrils, but does not establish a distinct structuring route that produces compact particles as an intended outcome. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

  • The same protein can form very different colloidal states depending on processing severity and chemical association.

    “These results illustrate that the same protein can form very different colloidal states depending on processing severity and chemical associ­ ation”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Mykolenko et al., 2024

    Section 3.4.6 (page unavailable) reports that amaranth fibril morphologies varied with incubation temperature and duration, supporting the processing-severity part of the claim. Section 3.4.4 discusses possible hydrogen-bond disruption during hydrolysis, but the paper does not establish chemical association as a separate determinant of the different colloidal states. (LLM, conf=0.83)

    Experimental — accuracy not yet measured

  • Nanoparticle formation or fibrillation further strengthens β-sheet signatures and fluorescence perturbations, consistent with more extensive aggregation and tighter intermolecular packing.

    “Nanoparticle for­ mation or fibrillation further strengthens β -sheet signatures and fluo­ rescence perturbations, consistent with more extensive aggregation and tighter intermolecular packing”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Mykolenko et al., 2024

    Sections 3.4.3 and 3.4.4 report increased thiazole-orange fluorescence and β-sheet-rich structures during amaranth protein fibrillation; sections 3.4.5–3.4.6 describe further aggregation and tighter twisting of fibrils. The cited paper does not establish the same changes for nanoparticle formation or show that they indicate tighter intermolecular packing. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

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Metadata

Authors
Mykolenko, S., Soon, W. L., & Mezzenga, R.
Affiliations
  • ETH Zurich (CH)
  • Nanyang Technological University (SG)
Corresponding author
  • Mykolenko, Svitlana
  • Mezzenga, Raffaele
ORCID
Venue
Food Hydrocolloids
Publisher
Elsevier BV
Published
2024-04
Volume
149
Pages
109604
ISSN
0268-005X (ISSN-L)
DOI
10.1016/j.foodhyd.2023.109604
OpenAlex
W4389271977
Cited by
60
References
0
Citations by year
2026: 26 · 2025: 21 · 2024: 13
FWCI
6.91
Type
journal article
Language
en
Open access
Licence
Locations
  • Food Hydrocolloids (publishedVersion, cc-by)
  • DR-NTU (Nanyang Technological University) (submittedVersion)
  • Repository for Publications and Research Data (ETH Zurich) (submittedVersion, cc-by)
  • ETH Zürich Research Collection
Funders
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Physical Sciences › Materials Science › Biomaterials › Supramolecular Self-Assembly in Materials
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
Amaranthus hypochondriacus, amyloid fibrils, protein self-assembly, 11S globulin, amyloidogenic regions, acid hydrolysis, fibril polymorphism, beta-sheet, protein unfolding, plant proteins

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