Choi Hyun Woo, Hahn Jungwoo, Kim Hyun-Seok, Choi Young Jin
Research Institute for Agriculture and Life Sciences, Seoul National University, 1 Gwanakro, Gwanakgu, Seoul 08826, Republic of Korea.
Department of Food and Nutrition, Duksung Women's University, 33 Samyang-Ro 144-Gil, Dobonggu, Seoul 01369, Republic of Korea.
Food Chem. 2025 Mar 15;468:142403. doi: 10.1016/j.foodchem.2024.142403. Epub 2024 Dec 7.
In this study, we used protein blends and rheological methods to simulate the structural changes in high-moisture meat analogs (HMMA) within the cooling die and clarified the complex interactions between changes in protein composition and HMMA's textural characteristics. Rheological analysis revealed a decrease in rheological parameters with an increase in the cooling die temperature, although no structural collapse was observed in gel stability. Although the hardness of HMMA decreased with an increase in the cooling die temperature, it facilitated the alignment of protein structures, resulting in an enhanced texturization index. Notably, this temperature increase led to a reduction in β-sheets and α-helix structures, which typically contributed to the stiffness and cohesion of protein networks, whereas β-turns increased, affecting the flexibility of proteins. Among the various chemical interactions, disulfide bonding uniquely increased at high temperatures, underscoring its critical role in the formation of fibrous structures.
在本研究中，我们使用蛋白质混合物和流变学方法来模拟高水分肉模拟物（HMMA）在冷却模具内的结构变化，并阐明了蛋白质组成变化与HMMA质地特性之间的复杂相互作用。流变学分析表明，随着冷却模具温度的升高，流变学参数降低，尽管在凝胶稳定性方面未观察到结构坍塌。尽管HMMA的硬度随着冷却模具温度的升高而降低，但它促进了蛋白质结构的排列，从而提高了纹理化指数。值得注意的是，温度升高导致β-折叠和α-螺旋结构减少，这些结构通常有助于蛋白质网络的刚度和凝聚力，而β-转角增加，影响了蛋白质的柔韧性。在各种化学相互作用中，二硫键在高温下独特地增加，突出了其在纤维结构形成中的关键作用。
