The Heat-Induced Gel–Sol Transition in Coated Tofu: A Study on Protein Conformation and Microstructural Changes

To enhance and stabilise the edible quality of coated tofu, this study explored the changes in the microstructure and intermolecular forces of coated tofu gel and sol under different heat treatments. It elucidated the phase transformation mechanism of coated tofu gel and sol under heat treatment. The results showed that the protein structure unfolded, the fluorescence intensity decreased, and the protein solubility, surface hydrophobicity, and free sulfhydryl group content increased as the coated tofu gel transformed to sol. Disulfide bonding and hydrophobic interactions were the primary intermolecular forces in the heat-induced gel-sol transition. FTIR showed that the content of β-sheets decreased significantly during gel-sol transformation, while the content of β-turns, α-helices and random coils increased significantly. Most remained relatively stable during the gel-sol transformation process, with only the A and B subunits of the 11S protein decreasing slightly. Their reduction became significant when the temperature reached 200 °C. Additionally, the high-temperature heat treatment promoted the gel-sol transition of the coated tofu, with its cross-section gradually transforming from a porous network structure to a more uniform and smooth texture during heat treatment process. The findings of this study provide a theoretical basis for improving the quality of coated tofu by optimising heat treatment parameters, laying the groundwork for future advancements in the development of pre-heat-treated coated tofu.

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Publication Details

Journal
Gels
Published
2025-03-24
DOI
https://doi.org/10.3390/gels11040237
Citations
3
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
3.49
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article

The Heat-Induced Gel–Sol Transition in Coated Tofu: A Study on Protein Conformation and Microstructural Changes

Ming Wen, Xin Xie, Xiaoli Diao, Shih-Wei Sun et al.
3 citations
Gels
Proteins in Food Systems
3.49
article

The Heat-Induced Gel–Sol Transition in Coated Tofu: A Study on Protein Conformation and Microstructural Changes

Ming Wen, Xin Xie, Xiaoli Diao, Shih-Wei Sun, Xiaolong Shen, Kuilin Zhang, Zhanrui Huang, Xiaohu Zhou, Hao Chen, Bin Li, Yang Li, Meng Li, Liangzhong Zhao, Ping Lv
article en
3 citations

Abstract

To enhance and stabilise the edible quality of coated tofu, this study explored the changes in the microstructure and intermolecular forces of coated tofu gel and sol under different heat treatments. It elucidated the phase transformation mechanism of coated tofu gel and sol under heat treatment. The results showed that the protein structure unfolded, the fluorescence intensity decreased, and the protein solubility, surface hydrophobicity, and free sulfhydryl group content increased as the coated tofu gel transformed to sol. Disulfide bonding and hydrophobic interactions were the primary intermolecular forces in the heat-induced gel-sol transition. FTIR showed that the content of β-sheets decreased significantly during gel-sol transformation, while the content of β-turns, α-helices and random coils increased significantly. Most remained relatively stable during the gel-sol transformation process, with only the A and B subunits of the 11S protein decreasing slightly. Their reduction became significant when the temperature reached 200 °C. Additionally, the high-temperature heat treatment promoted the gel-sol transition of the coated tofu, with its cross-section gradually transforming from a porous network structure to a more uniform and smooth texture during heat treatment process. The findings of this study provide a theoretical basis for improving the quality of coated tofu by optimising heat treatment parameters, laying the groundwork for future advancements in the development of pre-heat-treated coated tofu.

GelsVol. 11(4)
Northeast Agricultural University (CN), Shaoyang University (CN), Hunan Agricultural Products (China) (CN)
Clean water and sanitation
Openalex Percentile: Top 9%
Proteins in Food Systems
3.49
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