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

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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Publication Details

Journal
Journal of Agricultural and Food Chemistry
Published
2025-08-18
DOI
https://doi.org/10.1021/acs.jafc.5c07627
Citations
3
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
3.49
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article

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

Audrey L. Girard, Sanjana Sawant
3 citations
Journal of Agricultural and Food Chemistry
Proteins in Food Systems
3.49
article

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

Audrey L. Girard, Sanjana Sawant
article en
3 citations

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.

Journal of Agricultural and Food ChemistryVol. 73(36)
University of Wisconsin–Madison (US)
Zero hunger
Openalex Percentile: Top 8%
Proteins in Food Systems
3.49
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