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

• 食品工程 • 上一篇    

pH值偏移结合超声处理对鸡肝不溶蛋白乳化稳定性的影响

姚昕,姚敏,柳文哲,黄明远,赵圣明,郑海波,戚军,张春晖,黄明,熊国远   

  1. (1.安徽科技工程大学食品科学与工程学院,安徽省功能农业与功能食品重点实验室,安徽 滁州 239000;2.安徽农业大学食品与营养学院,农业农村部江淮农产品精深加工与资源利用重点实验室,安徽 合肥 230036;3.中国农业科学院农产品加工研究所,农业农村部农产品加工与贮藏重点实验室,北京 100193;4.南京农业大学食品科技学院,肉品质量控制与新资源创制全国重点实验室,江苏 南京 210095)
  • 发布日期:2026-07-02
  • 基金资助:
    国家自然科学基金面上项目(32372352);安徽省高校优秀科研创新团队项目(2024AH010007); 安徽科技工程大学科技创新团队项目(2023KJCXTD003)

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

摘要: 以畜禽副产物-新鲜鸡肝不溶蛋白为研究对象,采用pH值偏移结合超声处理后,通过测定鸡肝不溶蛋白粒径、Zeta电位、流变特性、乳化稳定性及乳析指数等指标,结合激光共聚焦观察,探究联合处理对其乳液稳定性的影响。结果表明:pH值偏移与超声的联合处理效果随pH值变化(pH 11.0~13.0)呈现“先上升后下降”的趋势,pH 11.0~12.0范围内,碱性增强可强化超声对蛋白聚集体的解离与乳液液滴细化效果,乳液稳定性持续优化;pH值超过12.0后,过度碱处理引发蛋白无序聚集,削弱超声的均质与蛋白结构调控作用,对超声效果的影响更清晰,即无序聚集的蛋白不仅会阻碍超声对油滴的均质破碎,还会影响超声诱导的蛋白结构舒展与界面吸附效果,最终导致乳化稳定性显著变差(P<0.05)。其中pH 12.0→5.5结合200 W超声处理,使乳液D4,3值显著降至(19.10±0.17)μm(P<0.05),Zeta电位绝对值达(32.3±0.9)mV,乳化活性与乳化稳定性显著增加(P<0.05),分别为(67.9±0.4)m2/g和(96.7±0.4)%、4 ℃贮藏76 h乳析指数极显著减少到(4.19±0.20)%(P<0.01),液滴呈规则球形且无团聚。研究结果为改性畜禽副产物不溶蛋白、改善其加工特性提供技术路径和理论依据,对推动鸡肝高值化利用具有重要意义。

关键词: 鸡肝不溶蛋白;pH值偏移结合超声处理;乳液稳定性;微观结构;宏观特性

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

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