The Emulsion Properties of Chicken Liver Protein Recovered through Isoelectric Solubilization/Precipitation Processes.

This study investigated the feasibility to improve the emulsifying capacity of chicken liver (CL) protein using different isoelectric solubilization/precipitation (ISP) processes. The CL proteins were first solubilized at alkaline pH 10.5, 11.0, 11.5, and 12.0, followed by precipitation at pH 5.0, 5.5, and 6.0, respectively. Fresh CL paste was set as the control (raw). With the increase in solubilization pH, the protein recovery yield increased under the same precipitation pH, and the pH 12.0, 5.5 treatment obtained the highest recovery yield of 82% (p < 0.05), followed by the pH 5.0 precipitation treatments and the pH 12.0, 6.0 treatment. The particle size distribution of D3,2 and D4,3 was smaller for the pH 10.5 (except for the D4,3 of pH 10.5, 5.0) and pH 11.0 solubilization treatments than those of the other treatments (p < 0.05), regardless of precipitation pH. Compared with that of the raw control, the emulsions of the pH 10.5 and pH 11.0 solubilization treatments, and pH 12.0, 6.0 treatment showed good stability. The pH 10.5, 6.0 treatment showed the best emulsification activity, followed by the pH 10.5, 5.5, pH 11.0, 6.0, pH 12.0, 6.0, pH 10.5, 5.0, pH 11.0, 5.5, and pH 11.0, 5.0 treatments, which were uniformly distributed and were stable without the stratification of emulsions. It was concluded that CL protein recovered through suitable ISP showed potential as an emulsifier, and thus expanded the application of CL protein for human consumption.