# Unravelling the Deterioration Mechanism of the Coated Tofu Gel During Cold Storage: The Role of Protein Oxidation

**Authors:** Saihua Sun, Xiaohu Zhou, Yang Liu, Xinrui Diao, Jian Zeng, Jie Chen, Fenfang Song, Xiangjun Li, Xiaojie Zhou, Hao Chen, Zhanrui Huang, Liangzhong Zhao, Dajun Yang, Xiangle Huang

PMC · DOI: 10.3390/gels12020173 · Gels · 2026-02-15

## TL;DR

This study explores how cold storage affects the quality of coated tofu by examining protein changes that lead to spoilage.

## Contribution

The study reveals how protein oxidation and structural changes during cold storage correlate with quality deterioration in coated tofu.

## Key findings

- Lower storage temperature (4°C) significantly slows protein oxidation and quality loss in coated tofu.
- Protein structural changes, including loss of α-helices and β-sheets, correlate with textural and color deterioration.
- Oxidative denaturation and structural reaggregation of proteins are key drivers of coated tofu spoilage during cold storage.

## Abstract

Coated tofu is prone to spoilage and degradation during processing, storage, and transportation. As the material basis for gel of coated tofu, proteins determine coated tofu’s unique qualities, such as its colour, flavour, and texture. This study aimed to investigate the changes in the quality of coated tofu and the physicochemical properties of its proteins during cold storage (4 °C and 10 °C, 14 days), as well as the intrinsic correlations between these variables. Quality deterioration and protein structural changes were significantly slower at 4 °C than at 10 °C, with lower temperature effectively delaying quality loss. The results indicated that as storage time increased, the freshness of coated tofu declined, its textural properties significantly deteriorated, and the protein gel network structure became impaired. Meanwhile, the proteins underwent significant oxidative denaturation, characterized by a decrease in the free thiol group content and an increase in surface hydrophobicity. The tertiary structure exhibited unfolding and disruption, while the secondary structure transitioned from an ordered to a disordered state. Specifically, the contents of α-helixes and β-sheets decreased significantly, reaching 34.96% and 8.68%, respectively, after 14 days of storage at 4 °C. In contrast, the contents of β-turns and random coils increased to 30.11% and 26.25%, respectively, under the same storage conditions. The subunit bands of the 11S and 7S proteins gradually weakened, and the protein structure tended to loosen. Correlation analysis revealed that the oxidative denaturation, structural depolymerization, and reaggregation of proteins were highly significantly correlated with the textural breakdown and colour deterioration of coated tofu, which together contributed to the quality degradation of coated tofu during cold storage. The findings of this study provide fundamental data and technical support for the development of cold storage methods for coated tofu.

## Linked entities

- **Proteins:** 11S (DNA segment, 11S)

## Full-text entities

- **Diseases:** injury to (MESH:D014947)
- **Chemicals:** fatty acids (MESH:D005227), malondialdehyde (MESH:D008315), amines (MESH:D000588), TCA (MESH:D014238), amino acids (MESH:D000596), nitrogen (MESH:D009584), EDTA (MESH:D004492), Sulfhydryl (MESH:D013438), aspartic acid (MESH:D001224), disulfide (MESH:D004220), Na2 (MESH:C033479), ammonia (MESH:D000641), acids (MESH:D000143), gold (MESH:D006046), sodium chloride (MESH:D012965), TBARS (-), sodium bicarbonate (MESH:D017693), hydrogen peroxides (MESH:D006861), sulfuric acid (MESH:C033158), ninhydrin (MESH:D009555), Glycine (MESH:D005998), ethanol (MESH:D000431), glutamic acid (MESH:D018698), HCl (MESH:D006851), hydrogen (MESH:D006859), SDS (MESH:D012967), tryptophan (MESH:D014364), PBS (MESH:D007854), glutaraldehyde (MESH:D005976), KBr (MESH:C039004), Thiobarbituric Acid (MESH:C029684), lipid (MESH:D008055), magnesium oxide (MESH:D008277), BCA (MESH:C047117), Water (MESH:D014867)
- **Species:** Homo sapiens (human, species) [taxon 9606], Glycine max (soybean, species) [taxon 3847]
- **Mutations:** C) for 10, G9800A

## Full text

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## Figures

8 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12940414/full.md

## References

47 references — full list in the complete paper: https://tomesphere.com/paper/PMC12940414/full.md

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Source: https://tomesphere.com/paper/PMC12940414