ArticleFood chemistry: X2022
The temporal evolution mechanism of structure and function of oxidized soy protein aggregates.
Article in Food chemistry: X, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Unravelling the Deterioration Mechanism of the Coated Tofu Gel During Cold Storage: The Role of Protein Oxidation.Gels (Basel, Switzerland) · 2026Article
- Time-dependent shifts in microbiota and metabolites of Yuba under ambient storage: implication for quality deterioration and spoilage.Frontiers in nutrition · 2026Article
- Characteristic of different thermal treatment-induced dough protein oxidation and its impact on human gut microbiota.Current research in food science · 2026Article
- Enhancing emulsification and gelation properties of porcine myofibrillar protein under low NaCl by lipoxygenase fromFood science and biotechnology · 2025Article
- Effects of Different Types of Starch on Physicochemical Properties and Microstructure of Beef during Cold Storage.Foods (Basel, Switzerland) · 2024Article
- Impact of Cavitation Jet on the Structural, Emulsifying Features and Interfacial Features of Soluble Soybean Protein Oxidized Aggregates.Foods (Basel, Switzerland) · 2023Article
- Lipid oxidation in foods and its implications on proteins.Frontiers in nutrition · 2023Review
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Authors and funding
9 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The emulsifying activity of soy protein would decrease after long-term storage, which caused huge economic losses to food processing plants. This study explored the temporal evolution mechanism of oxidation on the structure and function of soy protein aggregates, which would improve the application of soy protein in food industry. Decreased α-helix and increased random coil were observed at the initial oxidation stage (0-4 h), which induced increases in hydrophobicity and disulfide bond content. In addition, emulsibility increased significantly. However, when the oxidation time extended to 6-12 h, the soluble aggregates transformed into insoluble aggregates with large particle size, low solubility, and molecular flexibility. Surface hydrophobicity and emulsifying activity were reduced, resulting in bridging flocculation of emulsion droplets. Mutual transformation between components is affected by factors that include spatial conformation and intermolecular forces, which eventually lead to functional changes in the protein molecules.
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