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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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.
KeywordsPSE-like Isoelectric solubilization/precipitation Gelation properties Molecular force
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).
- Chen, Y. C., & Jaczynski, J. (2007). Protein recovery from rainbow trout (Oncorhynchus mykiss) processing byproducts via isoelectric solubilization/precipitation and its gelation properties as affected by functional additives. Journal of Agricultural & Food Chemistry, 55(22), 9079–9088.CrossRefGoogle Scholar
- Cortés-Ruiz, J. A., Pacheco-Aguilar, R., Lugo-Sánchez, M. E., Carvallo-Ruiz, M. G., & García-Sánchez, G. (2008). Production and functional evaluation of a protein concentrate from giant squid (Dosidicus gigas) by acid dissolution and isoelectric precipitation. Food Chemistry, 110(2), 486–492.CrossRefGoogle Scholar
- Cortés-Ruiz, J. A., Pacheco-Aguilar, R., Ramírez-Suárez, J. C., Lugo-Sánchez, M. E., García-Orozco, K. D., Sotelo-Mundo, R. R., & Peña-Ramos, A. (2015). Conformational changes in proteins recovered from jumbo squid (Dosidicus gigas) muscle through pH shift washing treatments. Food Chemistry, 196, 769–775.CrossRefGoogle Scholar
- Gornall, A. G., Bardawill, C. J., & David, M. M. (1949). Determination of serum proteins by means of the biuret reaction. Journal of Biological Chemistry, 177(2), 751–766.Google Scholar
- Kinsella, J. E. (1982). Relationship between structure and functional properties of food proteins. Food Proteins, 1, 51–103.Google Scholar
- Kristinsson, H. G. (2002). Conformational and functional changes of hemoglobin and myosin induced by pH: Functional role in fish quality. Doctoral dissertation. Morgantown: University of Massachusetts Amherst.Google Scholar
- Taskaya, L., Chen, Y. C., Beamer, S., & Jaczynski, J. (2009). Texture and colour properties of proteins recovered from whole gutted silver carp (Hypophthalmichthys molitrix) using isoelectric solubilisation/precipitation. Journal of the Science of Food & Agriculture, 89(2), 349–358.CrossRefGoogle Scholar
- Zhao, X., Chen, X., Han, M. Y., Qian, C., Xu, X. L., & Zhou, G. H. (2016a). Application of isoelectric solubilization/precipitation processing to improve gelation properties of protein isolated from pale, soft, exudative (PSE)-like chicken breast meat. LWT - Food Science and Technology, 72, 141–148.CrossRefGoogle Scholar
- Zhao, X., Zou, Y. F., Shao, J. J., Chen, X., Han, M. Y., & Xu, X. L. (2016b). Comparison of the acidic and alkaline treatment on emulsion composite gel properties of the proteins recovered from chicken breast by isoelectric solubilization/precipitation process. Journal of Food Processing & Preservation. doi: 10.1111/jfpp. 12884.Google Scholar