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

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

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Article in Foods (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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8 authors.

Yaozu GuoCollege of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China.

Jiaxuan HanCollege of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China.

Boxing YinCollege of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China.

Ruixia GuCollege of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China.

Dawei ChenCollege of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China.ORCID 0000-0003-0423-0586

Zhangwei HeShaanxi Key Laboratory of Environmental Engineering, School of Environmental and Municipal Engineering, Xi'an University of Architecture and Technology, Xi'an 710055, China.

Congcong TangShaanxi Key Laboratory of Environmental Engineering, School of Environmental and Municipal Engineering, Xi'an University of Architecture and Technology, Xi'an 710055, China.

Wenqiong WangCollege of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China.

Funding

Jiangsu Province Dairy Bioengineering Technology Research Center open project KYRY2023017Key Laboratory of Probiotics and Dairy Deep Processing of Yangzhou YZ2020265Major Project of Higher Education Institutions in Jiangsu Province 25KJA550003Sichuan Province science and Technology plan "unveiled" project 2023YFN0101This work was funded by Key Laboratory of Membrane Separation of Shaanxi Province 2022MFL02

6 · The paper itself

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.

Indexed as

antioxidant capacityconformational changefermentationoxidative stabilitysoybean 11S protein

Identifiers

PMID41596798

DOI10.3390/foods15020199

PMCPMC12840035

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