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Changes of Molecular Forces During Thermo-Gelling of Protein Isolated from PSE-Like Chicken Breast by Various Isoelectric Solubilization/Precipitation Extraction Strategies

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Abstract

Changes in protein intermolecular interactions during thermo-gelling were measured to compare the gelation properties of isoelectric solubilization/precipitation (ISP)-isolated protein extracted (solubilized at 3.5 and 11.0, precipitated at 5.5 and 6.2) from pale, soft, and exudative (PSE)-like chicken breast meat with raw meat paste. The solubility of both in water and salt (0.6 M NaCl) decreased significantly after ISP treatments. Protein profile analysis revealed that precipitation pH showed little influence on protein profile. Under pH 3.5 and pH 11.0 solubility conditions, the recovered protein at pH 6.2 showed significantly higher gel hardness than that at pH 5.5, which can be induced by hydrophobic change. Surface hydrophobicity (SH0) and hydrophobic interactions at 25 °C presented similar results, indicating that the soluble protein at pH 11.0 exhibited a higher value after precipitation at pH 6.2 than that at pH 5.5, and the hydrophobicity of pH 3.5 isolates was higher than that of the pH 11.0 groups. However, the maximum hydrophobicity upon heating was inconsistent with initial tendencies. Given that the hydrophobic residues were exposed sufficiently during the ISP process, the ISP-treated proteins, particularly the samples extracted at pH 3.5, might be less susceptible to heat-induced exposure. The gelation behavior of the ISP-treated proteins had been modified on the basis of the intermolecular bonds during heating. In conclusion, the precipitation condition demonstrated excellent relevance for product development based on functionality.

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Acknowledgements

This research was supported by the China Agriculture Research System (CARS-42) funded by the Chinese Ministry of Agriculture and the National Natural Science Foundation of China (No. 31571854).

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Authors and Affiliations

  1. Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, Key Laboratory of Animal Products Processing, MOA, Key Lab of Meat Processing and Quality Control, MOE, College of Food Science and Technology, Nanjing Agricultural University, Nanjing, 210095, People’s Republic of China

    Xue Zhao, Tong Xing, Xing Chen, Minyi Han, Shaolin Deng, Xinglian Xu & Guanghong Zhou

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  1. Xue Zhao
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  2. Tong Xing
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  3. Xing Chen
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  4. Minyi Han
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  5. Shaolin Deng
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  6. Xinglian Xu
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  7. Guanghong Zhou
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Correspondence to Xinglian Xu.

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A Project Funded by the Priority Academic Program Development of Jiangsu Higher Education Institutions

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Zhao, X., Xing, T., Chen, X. et al. Changes of Molecular Forces During Thermo-Gelling of Protein Isolated from PSE-Like Chicken Breast by Various Isoelectric Solubilization/Precipitation Extraction Strategies. Food Bioprocess Technol 10, 1240–1247 (2017). https://doi.org/10.1007/s11947-017-1893-4

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  • DOI: https://doi.org/10.1007/s11947-017-1893-4

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