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Modification of Soybean 11S Protein by Fermentation: Antioxidant Capacity, Oxidative Stability in Emulsions and
Yaozu Guo1, Jiaxuan Han1, Boxing Yin1
1College of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China.
Foods (Basel, Switzerland)
|January 28, 2026
Summary
Fermentation enhances soybean 11S protein (F11S) bioactivity, peaking at 16 hours. A stable, refolded structure at 16 hours, not hydrophobicity, drives superior antioxidant and emulsion stability.
Area of Science:
- Food Science
- Protein Chemistry
- Biochemistry
Background:
- Fermentation effectively enhances plant protein bioactivity.
- The relationship between fermented soybean 11S protein (F11S) structure and function needs further investigation.
Purpose of the Study:
- Evaluate the antioxidative efficacy and emulsion application of F11S.
- Investigate the structural evolution of F11S during fermentation.
- Determine the key structural factors responsible for enhanced functionality.
Main Methods:
- Fermentation of soybean 11S protein.
- Antioxidant activity assays (·OH and DPPH radical scavenging).
- Emulsion stability testing.
- Structural analysis (surface hydrophobicity, refolding assessment).
Main Results:
- F11S bioactivity peaked at 16 hours of fermentation.
- Maximal ·OH (84.51%) and DPPH (93.84%) radical scavenging observed at 16 hours.
- F11S-16h showed superior emulsion oxidative stability (lowest peroxide value: 4.33 mmol/kg).
- Protein unfolding peaked at 12 hours, followed by refolding into a stable conformation at 16 hours.
Conclusions:
- Fermentation time critically influences F11S bioactivity and structure.
- The stable refolded conformation at 16 hours, not peak hydrophobicity, dictates superior antioxidant and emulsion stabilizing properties.
- This study clarifies the structure-function relationship of F11S, optimizing its application in food systems.
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