# Modification of Soybean 11S Protein by Fermentation: Antioxidant Capacity, Oxidative Stability in Emulsions and Structural Evolution

**Authors:** Yaozu Guo, Jiaxuan Han, Boxing Yin, Ruixia Gu, Dawei Chen, Zhangwei He, Congcong Tang, Wenqiong Wang

PMC · DOI: 10.3390/foods15020199 · Foods · 2026-01-07

## TL;DR

Fermenting soybean 11S protein for 16 hours improves its antioxidant activity and stability in emulsions due to a stable protein structure.

## Contribution

The study reveals that a refolded protein structure, not just hydrophobicity, determines the enhanced functionality of fermented soybean 11S protein.

## Key findings

- Fermented soybean 11S protein at 16 h showed highest ·OH and DPPH radical scavenging capacities.
- The 16 h fraction had the lowest peroxide value in emulsions after 15 days of storage.
- Extended fermentation induced a refolding process leading to a thermodynamically stable protein conformation.

## Abstract

Fermentation is an effective method to enhance the bioactivity of plant proteins, yet the link between the functionality and conformational state of fermented soybean 11S protein (F11S) requires clarification. This study first evaluated the antioxidative efficacy of F11S and its application in emulsion systems, followed by a mechanistic investigation into its structural evolution. Results showed that the bioactivity of F11S was strictly fermentation-time-dependent, reaching its peak at 16 h. At this stage, F11S exhibited maximal scavenging capacities for ·OH (84.51 ± 2.53%) and DPPH radicals (93.84 ± 2.62%). Crucially, in a Tween 20 emulsion system, the F11S-16h fraction demonstrated superior oxidative stability, maintaining the lowest peroxide value (4.33 ± 0.53 mmol/kg) after 15 days of storage. To elucidate the mechanism behind this enhanced functionality, structural analysis was conducted. It revealed that while surface hydrophobicity peaked at 12 h due to protein unfolding, extended fermentation to 16 h induced a refolding process, guiding the protein into a thermodynamically stable conformation. These findings indicate that the stable refolded structure formed at 16 h, rather than maximal hydrophobicity, is the key determinant for the superior antioxidant performance and emulsion stabilizing ability of F11S.

## Linked entities

- **Chemicals:** Tween 20 (PubChem CID 443314), ·OH (PubChem CID 961)

## Full-text entities

- **Chemicals:** OH (MESH:C031356), Tween 20 (MESH:D011136), peroxide (MESH:D010545), -16h (-)
- **Mutations:** 11S, F11S

## Full text

_Full body text omitted from this summary view._ Fetch the complete paper as Markdown: https://tomesphere.com/paper/PMC12840035/full.md

## Figures

8 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12840035/full.md

## References

40 references — full list in the complete paper: https://tomesphere.com/paper/PMC12840035/full.md

---
Source: https://tomesphere.com/paper/PMC12840035