State Key Laboratory of Food Science and Resources, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
State Key Laboratory of Food Science and Resources, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, USA.
Food Chem. 2024 Oct 15;455:139870. doi: 10.1016/j.foodchem.2024.139870. Epub 2024 May 28.
The present study investigated thermal gelation of mixed sarcoplasmic (Sarc), myofibrillar (Myof), and pea proteins corresponding to partial meat replacements (0, 25, and 50%) by pea protein isolate (PPI) at reducing salt levels (0.6 → 0.1 M NaCl) to understand in situ (simulated) structure-forming properties of hybrid meat analogues. The amount of soluble proteins in hybrids generally increased with salt concentrations and PPI substitution. While muscle proteins (mixed Sarc and Myof) had the strongest gelling capacity, hybrid proteins also exhibited moderate aggregation and gelling activity based on the sol→gel rheological transition and gel hardness testing. Sarc and pea 7S/11S globulins collectively compensated for the attenuated gelling capacity of mixed proteins due to diminishing Myof in the hybrids. Immobilized water within hybrid protein gels was tightly bonded (T from nuclear magnetic resonance), consistent with the dense and uniform microstructure observed. These findings offer a new knowledge base for developing reduced-salt hybrid meat analogues.
本研究通过豌豆分离蛋白（PPI）在低盐水平（0.6→0.1 M NaCl）下替代部分肉类（0、25 和 50%），对混合肌浆（Sarc）、肌原纤维（Myof）和豌豆蛋白的热凝胶化进行了研究，以了解混合肉模拟物的原位（模拟）结构形成特性。混合物中的可溶性蛋白质的含量通常随着盐浓度和 PPI 替代量的增加而增加。虽然肌肉蛋白（混合的 Sarc 和 Myof）具有最强的凝胶形成能力，但基于溶胶→凝胶流变转变和凝胶硬度测试，混合蛋白也表现出中等程度的聚集和凝胶化活性。由于混合蛋白中肌球蛋白的减少，Sarc 和豌豆 7S/11S 球蛋白共同补偿了混合蛋白凝胶形成能力的减弱。混合蛋白凝胶中固定的水是紧密结合的（来自核磁共振的 T），与观察到的致密和均匀的微观结构一致。这些发现为开发低盐混合肉模拟物提供了新的知识库。
