Institute of Food Science and Technology CAAS, Comprehensive Utilization Laboratory of Cereal and Oil Processing, Ministry of Agriculture and Rural Affairs, Beijing 100193, China.
Wilmar Biotechnology Research and Development Center Company Limited, Shanghai 200000, China.
Int J Biol Macromol. 2024 Jul;273(Pt 1):132911. doi: 10.1016/j.ijbiomac.2024.132911. Epub 2024 Jun 4.
The texture of soybean protein-based products is primarily influenced by the aggregation and gel morphology of the protein, which is modulated by manufacturing factors. Interactions involved in protein morphology changes include disulfide bonds, hydrophobic interactions, electrostatic interactions, and hydrogen bonds. Notably, an interaction perspective probably provides a new way to explaining the aggregation and gel morphology, which could help overcome the hurdle of developing a textured product. Based on the interaction perspective, this review provides detailed information and evidence on aggregation, conformational stability, and gel network morphology of soybean protein and its components induced by pH, NaCl, and temperature. pH-induced electrostatic interactions and hydrogen bonds, NaCl-induced electrostatic interactions, and temperature-induced hydrophobic interactions and disulfide linkages are the main motivations responsible for changes in soybean aggregation and gel morphology. By reducing the proportion of strong-interactions, such as disulfide linkages and hydrophobic interactions, and increasing the proportion of weak-interactions, such as electrostatic interactions and hydrogen bonds, the protein total surface area expands, indicating increased conformational stretching and decreased cohesion. This possibly results in reduced hardness and increased toughness of textured proteins. The opposite effect can be observed when the proportion of strong interactions is increased and that of weak interactions is decreased.
大豆蛋白基产品的质地主要受蛋白质的聚集和凝胶形态的影响，而这些又受到制造因素的调节。涉及蛋白质形态变化的相互作用包括二硫键、疏水相互作用、静电相互作用和氢键。值得注意的是，相互作用的观点可能为解释聚集和凝胶形态提供了一种新的方法，这有助于克服开发质地产品的障碍。基于相互作用的观点，本文综述了 pH 值、NaCl 和温度对大豆蛋白及其组分的聚集、构象稳定性和凝胶网络形态的影响。pH 值诱导的静电相互作用和氢键、NaCl 诱导的静电相互作用以及温度诱导的疏水相互作用和二硫键是导致大豆聚集和凝胶形态变化的主要原因。通过减少二硫键和疏水相互作用等强相互作用的比例，增加静电相互作用和氢键等弱相互作用的比例，蛋白质的总表面积扩大，表明构象伸展增加，内聚性降低。这可能导致质地蛋白的硬度降低，韧性增加。相反，如果强相互作用的比例增加，弱相互作用的比例降低，则会产生相反的效果。
