Abstract：
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 (T2 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.
摘要：
本研究调查了混合肌浆（arc）的热凝胶化，肌原纤维（Myof），和豌豆蛋白对应于豌豆蛋白分离物（PPI）在降低盐水平（0.6→0.1MNaCl）下的部分肉类替代品（0、25和50％），以了解杂交肉类似物的原位（模拟）结构形成特性。杂合物中可溶性蛋白质的量通常随着盐浓度和PPI取代而增加。虽然肌肉蛋白（混合的Sarc和Myof）具有最强的胶凝能力，根据溶胶→凝胶流变转变和凝胶硬度测试，杂化蛋白还表现出中等的聚集和胶凝活性。由于杂种中Myof的减少，Sarc和豌豆7S/11S球蛋白共同补偿了混合蛋白质的胶凝能力减弱。杂合蛋白凝胶内的固定化水紧密结合（核磁共振的T2），与观察到的致密均匀的微观结构一致。这些发现为开发低盐混合肉类似物提供了新的知识库。
