开发具有所需营养和流变特性的预期动植物二元蛋白质系统是食品工业中重要且具有挑战性的追求。我们对添加盐对食物蛋白质聚集行为的影响的理解目前基于单一模型蛋白质系统,然而,这种知识是相当有限的二元蛋白质系统。在这里,各种离子强度设置用于减轻热过程中豌豆-鳕鱼混合蛋白之间的排斥力,这进一步有利于加强凝胶网络的建设。透射电子显微镜(TEM)和动态光散射(DLS)共同表明,形成了较大的热诱导蛋白聚集体,随着离子强度的增加,其尺寸增加。在存在2.5mMCaCl2和50mMNaCl的情况下,二硫键从19.3增加到27.53和30.5μM/g,分别。值得注意的是,当引入2.5mMCaCl2或25mMNaCl时,可以发现类似的聚集行为,由于Ca2+与蛋白质的特异性结合增强了聚集趋势。与增强的蛋白质分子之间的交联相关,盐赋予复合凝胶具有较好的胶凝性能,通过增加的储能模量证明。此外,在升高的离子强度下,混合蛋白质的胶凝温度降至50°C以下。同时,添加5.0mMCaCl2和100mMNaCl后,复合凝胶中网络蛋白的比例从82.05%显着增加到93.61%和92.31%,分别。这些发现为设计经济上可行且面向健康的动植物二元蛋白质系统提供了宝贵的基础。
Developing prospective plant-animal binary protein systems with desirable nutritional and rheological properties stands as a significant and challenging pursuit within the food industry. Our understanding of the effect of adding salt on the aggregation behavior of food proteins is currently based on single model protein systems, however, this knowledge is rather limited following binary protein systems. Herein, various ionic strength settings are used to mitigate the repulsive forces between pea-cod mixed proteins during the thermal process, which further benefits the construction of a strengthened gel network. Transmission electron microscopy (TEM) and dynamic light scattering (DLS) collectively demonstrated that larger heat-induced protein aggregates were formed, which increased in size with higher ionic strength. In the presence of 2.5 mM CaCl2 and 50 mM NaCl, the disulfide bonds significantly increased from 19.3 to 27.53 and 30.5 μM/g, respectively. Notably, similar aggregation behavior could be found when introducing 2.5 mM CaCl2 or 25 mM NaCl, due to the enhanced aggregation tendency by specific binding of Ca2+ to proteins. With relevance to the strengthened cross-links between protein molecules, salt endowed composite gels with preferable gelling properties, evidenced by increased storage modulus. Additionally, the gelling temperature of mixed proteins decreased below 50 °C at elevated ionic strength. Simultaneously, the proportion of network proteins in composite gels increased remarkably from 82.05 % to 93.61 % and 92.31 % upon adding 5.0 mM CaCl2 and 100 mM NaCl, respectively. The findings provide a valuable foundation for designing economically viable and health-oriented plant-animal binary protein systems.