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Cited by 14Proteins in Food SystemsPolysaccharides Composition and ApplicationsSilk-based biomaterials and applications

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Complexation with Ionic Polysaccharides Mitigates pH-Dependent Degradation of Soy Protein Fibril Structure and Functionality

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Sawant, Sanjana, Girard, Audrey L.·2025·Journal of Agricultural and Food Chemistry
DOI 10.1021/acs.jafc.5c07627PMC PMC12503362
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Abstract

This study explored complexation of soy protein fibrils with gellan gum (anionic) and chitosan (cationic) to mitigate pH-induced degradation of fibril structure and function. Unfibrillated proteins combined with polysaccharides were studied as controls. Chitosan complexation preserved fibril integrity, with a moderate particle size increase (∼2.5x) and AFM imaging of fibrils alongside some aggregates when pH was increased from 2 to 4. FTIR analysis confirmed that chitosan best preserved the fibril β-sheet structure, primarily through electrostatic interactions. A Rapid Visco Analyzer study revealed that chitosan-modified fibrils retained their gelling ability at pH 4 (final viscosity ≈ 115 cP), comparable to fibrils at pH 2 (∼93 cP). Gellan gum complexation resulted in the formation of self-supporting gels at pH 7 (final viscosity ≈ 688 cP), likely due to electrostatic repulsion between like-charged components. Overall, this work provides valuable insights into mitigating pH-induced fibril degradation, thus expanding the potential applications of protein fibrils in food matrices.

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1 (A) Particle size and (B) ζ-potential of fibrillated protein samples analyzed using dynamic light scattering. SPF = fibrillated soy protein; GF = fibrillated soy protein with gellan gum; CF = fibrillated soy protein with chitosan. Letters denote significant differences across all samples (p < 0.05).
1 (A) Particle size and (B) ζ-potential of fibrillated protein samples analyzed using dynamic light scattering. SPF = fibrillated soy protein; GF = fibrillated soy protein with gellan gum; CF = fibrillated soy protein with chitosan. Letters denote significant differences across all samples (p < 0.05).CC BY · PubMed Central
2 Surface hydrophobicity (H0) of soy protein samples quantified using the hydrophobic fluorescent probe, ANS. SP = unfibrillated soy protein; GG = unfibrillated soy protein with gellan gum; CT = unfibrillated soy protein with chitosan; SPF = fibrillated soy protein; GF = fibrillated soy protein with gellan gum; CF = fibrillated soy protein with chitosan. Letters denote significant differences across all samples (p < 0.05).
2 Surface hydrophobicity (H0) of soy protein samples quantified using the hydrophobic fluorescent probe, ANS. SP = unfibrillated soy protein; GG = unfibrillated soy protein with gellan gum; CT = unfibrillated soy protein with chitosan; SPF = fibrillated soy protein; GF = fibrillated soy protein with gellan gum; CF = fibrillated soy protein with chitosan. Letters denote significant differences across all samples (p < 0.05).CC BY · PubMed Central
3 SDS-PAGE profiles of different samples separated under nonreducing conditions. Lanes are labeled by sample code: M = molecular weight marker; SP2/4/7 = unfibrillated soy protein at pH 2, 4, or 7; GG2/4/7 = unfibrillated soy protein with gellan gum at pH 2, 4, or 7; CT2/4/7 = unfibrillated soy protein with chitosan at pH 2, 4, or 7; SPF2/4/7 = fibrillated soy protein at pH 2, 4, or 7; GF2/4/7 = fibrillated soy protein with gellan gum at pH 2, 4, or 7; CF2/4/7 = fibrillated soy protein with chitosan at pH 2, 4, or 7, respectively. The bands representing the subunits of β-conglycinin (7S) and glycinin (11S) soy globulins are labeled on the right side of the electrophoretogram.
3 SDS-PAGE profiles of different samples separated under nonreducing conditions. Lanes are labeled by sample code: M = molecular weight marker; SP2/4/7 = unfibrillated soy protein at pH 2, 4, or 7; GG2/4/7 = unfibrillated soy protein with gellan gum at pH 2, 4, or 7; CT2/4/7 = unfibrillated soy protein with chitosan at pH 2, 4, or 7; SPF2/4/7 = fibrillated soy protein at pH 2, 4, or 7; GF2/4/7 = fibrillated soy protein with gellan gum at pH 2, 4, or 7; CF2/4/7 = fibrillated soy protein with chitosan at pH 2, 4, or 7, respectively. The bands representing the subunits of β-conglycinin (7S) and glycinin (11S) soy globulins are labeled on the right side of the electrophoretogram.CC BY · PubMed Central
4 ThT fluorescence spectroscopy of soy protein samples modified with fibrillation and polysaccharide addition under different pH conditions. SP = unfibrillated soy protein; GG = unfibrillated soy protein with gellan gum; CT = unfibrillated soy protein with chitosan; SPF = fibrillated soy protein; GF = fibrillated soy protein with gellan gum; CF = fibrillated soy protein with chitosan. Uppercase and lowercase letters denote significant differences (p < 0.05) across the unfibrillated and fibrillated samples, respectively.
4 ThT fluorescence spectroscopy of soy protein samples modified with fibrillation and polysaccharide addition under different pH conditions. SP = unfibrillated soy protein; GG = unfibrillated soy protein with gellan gum; CT = unfibrillated soy protein with chitosan; SPF = fibrillated soy protein; GF = fibrillated soy protein with gellan gum; CF = fibrillated soy protein with chitosan. Uppercase and lowercase letters denote significant differences (p < 0.05) across the unfibrillated and fibrillated samples, respectively.CC BY · PubMed Central
5 Molecular interactions studied by solubilizing samples in different reagents. (A) Samples at pH 2; (B) samples at pH 4; and (C) samples at pH 7. Unfibrillated soy protein at pH 2, 4, 7 = SP2/4/7; unfibrillated soy protein with gellan gum at pH 2, 4, 7 = GG2/4/7; unfibrillated soy protein with chitosan at pH 2, 4, 7 = CT2/4/7, respectively. Fibrillated soy protein at pH 2, 4, 7 = SPF2/4/7; fibrillated soy protein with gellan gum at pH 2, 4, 7 = GF2/4/7; fibrillated soy protein with chitosan at pH 2, 4, 7 = CF2/4/7, respectively. Letters denote significant differences between samples at the same pH treated with the same reagent (p < 0.05).
5 Molecular interactions studied by solubilizing samples in different reagents. (A) Samples at pH 2; (B) samples at pH 4; and (C) samples at pH 7. Unfibrillated soy protein at pH 2, 4, 7 = SP2/4/7; unfibrillated soy protein with gellan gum at pH 2, 4, 7 = GG2/4/7; unfibrillated soy protein with chitosan at pH 2, 4, 7 = CT2/4/7, respectively. Fibrillated soy protein at pH 2, 4, 7 = SPF2/4/7; fibrillated soy protein with gellan gum at pH 2, 4, 7 = GF2/4/7; fibrillated soy protein with chitosan at pH 2, 4, 7 = CF2/4/7, respectively. Letters denote significant differences between samples at the same pH treated with the same reagent (p < 0.05).CC BY · PubMed Central
6 AFM images (5 × 5 μm) of fibrillated samples with and without addition of polysaccharides. Fibrillated soy protein at pH 2, 4, 7 = SPF2/4/7; fibrillated soy protein with gellan gum at pH 2, 4, 7 = GF2/4/7; fibrillated soy protein with chitosan at pH 2, 4, 7 = CF2/4/7, respectively.
6 AFM images (5 × 5 μm) of fibrillated samples with and without addition of polysaccharides. Fibrillated soy protein at pH 2, 4, 7 = SPF2/4/7; fibrillated soy protein with gellan gum at pH 2, 4, 7 = GF2/4/7; fibrillated soy protein with chitosan at pH 2, 4, 7 = CF2/4/7, respectively.CC BY · PubMed Central
7 SEM images of fibrillated samples with and without addition of polysaccharides. Fibrillated soy protein at pH 2, 4, 7 = SPF2/4/7; fibrillated soy protein with gellan gum at pH 2, 4, 7 = GF2/4/7; fibrillated soy protein with chitosan at pH 2, 4, 7 = CF2/4/7, respectively. Scale bar = 400 nm. Magnification = 21K X.
7 SEM images of fibrillated samples with and without addition of polysaccharides. Fibrillated soy protein at pH 2, 4, 7 = SPF2/4/7; fibrillated soy protein with gellan gum at pH 2, 4, 7 = GF2/4/7; fibrillated soy protein with chitosan at pH 2, 4, 7 = CF2/4/7, respectively. Scale bar = 400 nm. Magnification = 21K X.CC BY · PubMed Central
8 Flow behavior of different samples measured using the RVA. (A) Unfibrillated and fibrillated soy protein at pH 2, 4, 7 = SP2/4/7 and SPF2/4/7, respectively; (B) unfibrillated and fibrillated soy protein with chitosan at pH 2, 4, 7 = CT2/4/7 and CF2/4/7, respectively; (C) unfibrillated and fibrillated soy protein with gellan gum at pH 2, 4, 7 = GG2/4/7 and GF2/4/7, respectively. (D) Magnified view of the gellan gum–treatment graph to better visualize the GG2, GG4, GF2, and GF4 samples.
8 Flow behavior of different samples measured using the RVA. (A) Unfibrillated and fibrillated soy protein at pH 2, 4, 7 = SP2/4/7 and SPF2/4/7, respectively; (B) unfibrillated and fibrillated soy protein with chitosan at pH 2, 4, 7 = CT2/4/7 and CF2/4/7, respectively; (C) unfibrillated and fibrillated soy protein with gellan gum at pH 2, 4, 7 = GG2/4/7 and GF2/4/7, respectively. (D) Magnified view of the gellan gum–treatment graph to better visualize the GG2, GG4, GF2, and GF4 samples.CC BY · PubMed Central
9 (A) Samples before and after RVA treatment analyzed for phase separation after overnight storage in refrigerated conditions. (B) Inversion of samples stored overnight after RVA treatment to assess the formation of self-supporting gels. Unfibrillated soy protein at pH 2, 4, 7 = SP2/4/7; unfibrillated soy protein with gellan gum at pH 2, 4, 7 = GG2/4/7; unfibrillated soy protein with chitosan at pH 2, 4, 7 = CT2/4/7, respectively. Fibrillated soy protein at pH 2, 4, 7 = SPF2/4/7; fibrillated soy protein with gellan gum at pH 2, 4, 7 = GF2/4/7; fibrillated soy protein with chitosan at pH 2, 4, 7 = CF2/4/7, respectively.
9 (A) Samples before and after RVA treatment analyzed for phase separation after overnight storage in refrigerated conditions. (B) Inversion of samples stored overnight after RVA treatment to assess the formation of self-supporting gels. Unfibrillated soy protein at pH 2, 4, 7 = SP2/4/7; unfibrillated soy protein with gellan gum at pH 2, 4, 7 = GG2/4/7; unfibrillated soy protein with chitosan at pH 2, 4, 7 = CT2/4/7, respectively. Fibrillated soy protein at pH 2, 4, 7 = SPF2/4/7; fibrillated soy protein with gellan gum at pH 2, 4, 7 = GF2/4/7; fibrillated soy protein with chitosan at pH 2, 4, 7 = CF2/4/7, respectively.CC BY · PubMed Central

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Metadata

Authors
Sawant, S., & Girard, A. L.
Affiliations
University of Wisconsin–Madison (US)
Corresponding author
Girard, Audrey L.
ORCID
Venue
Journal of Agricultural and Food Chemistry
Publisher
American Chemical Society (ACS)
Published
2025-08-18
Volume
73
Issue
36
Pages
22734-22745
ISSN
  • 0021-8561 (ISSN-L)
  • 1520-5118
DOI
10.1021/acs.jafc.5c07627
PMC
PMC12503362
OpenAlex
W4413289162
Cited by
14
References
0
Citations by year
2026: 13 · 2025: 1
FWCI
6.61
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Agricultural and Food Chemistry (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by)
Funders
USDA Soybean and Nitrogen Fixation Research Unit at Raleigh, NC
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
  • Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
Keywords
gellan gum, chitosan, beta-sheet, electrostatic interactions, gelling ability, viscosity, protein self-assembly, food gels
MeSH terms
Hydrogen-Ion Concentration, Particle Size, Polysaccharides, Polysaccharides, Bacterial, Viscosity, Spectroscopy, Fourier Transform Infrared, Soybean Proteins, Chitosan

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CoChat. (2026). Citation check: Complexation with Ionic Polysaccharides Mitigates pH-Dependent Degradation of Soy Protein Fibril Structure and Functionality. https://app.cochat.ai/papers/10.1021/acs.jafc.5c07627
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Sawant, S., & Girard, A. L. (2025). Complexation with Ionic Polysaccharides Mitigates pH-Dependent Degradation of Soy Protein Fibril Structure and Functionality. Journal of Agricultural and Food Chemistry. https://doi.org/10.1021/acs.jafc.5c07627