FOOD SCIENCE ›› 2026, Vol. 47 ›› Issue (11): 225-233.doi: 10.7506/spkx1002-6630-20251128-240

• Food Engineering • Previous Articles    

Effect of pH-Shifting Combined with Ultrasonic Treatment on the Emulsion Stability of Insoluble Proteins from Chicken Liver

YAO Xin, YAO Min, LIU Wenzhe, HUANG Mingyuan, ZHAO Shengming, ZHENG Haibo, QI Jun, ZHANG Chunhui, HUANG Ming, XIONG Guoyuan   

  1. (1. Anhui Province Key Laboratory of Functional Agriculture and Functional Food, College of Food Science and Engineering, Anhui Science and Technology University, Chuzhou 239000, China; 2. Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization, Ministry of Agriculture and Rural Affairs, School of Food and Nutrition, Anhui Agricultural University, Hefei 230036, China; 3. Key Laboratory of Agro-products Processing and Storage, Ministry of Agriculture and Rural Affairs, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China; 4. State Key Laboratory of Meat Quality Control and New Resource Development, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China)
  • Published:2026-07-02

Abstract: This study investigated the effect of pH-shifting combined with ultrasonic treatment on the emulsion stability of insoluble proteins isolated from fresh chicken liver, a poultry by-product. The prepared emulsion samples were evaluated for particle size, zeta potential, rheological properties, emulsion stability, and creaming index and were observed by laser confocal microscopy. Results indicated that the synergistic effect of pH-shifting and ultrasonication exhibited an increasing then decreasing trend with pH variation (pH 11.0–13.0). Increasing pH from 11.0 to 12.0 promoted the dissociation of protein aggregates and reduced the size of emulsion droplets, leading to continuous optimization of emulsion stability. Beyond pH 12.0, excessive alkaline treatment induced disordered protein aggregation, which not only impeded ultrasonic fragmentation of oil droplets but also disrupted ultrasonically induced protein unfolding and interfacial adsorption, ultimately causing significant deterioration in emulsion stability (P < 0.05). Specifically, pH-shifting from 12.0 to 5.5 combined with 200 W ultrasonication significantly reduced the D4,3 value of emulsions to (19.10 ± 0.17) μm (P < 0.05), with the absolute value of the zeta potential reaching (32.3 ± 0.9) mV. Moreover, the combined treatment significantly increased the emulsifying activity index (EAI) and emulsion stability index (ESI) to (67.9 ± 0.4) m2/g and (96.7 ± 0.4)%, respectively (P < 0.05) and reduced the creaming index after 76 h storage at 4 ℃ to (4.19 ± 0.20)% (P < 0.01). The resulting emulsion droplets exhibited a regular spherical morphology without agglomeration. These findings provide a technical pathway and theoretical basis for modifying insoluble proteins in livestock and poultry by-products to enhance their processing characteristics, and hold significant implications for advancing the high-value utilization of chicken liver.

Key words: chicken liver insoluble proteins; pH-shifting combined with ultrasonic treatment; emulsion stability; microstructure; macro-properties

CLC Number: