Rutigliano Mariacinzia, Liberatore Maria Teresa, Dilucia Flavia, Quinto Maurizio, Kacmaz Sibel, Di Luccia Aldo, la Gatta Barbara
Department of Sciences of Agriculture, Food, Natural Resources and Engineering (DAFNE), University of Foggia, Via Napoli, 25, 71122 Foggia, Italy.
Department of Food Engineering, Engineering Faculty, Giresun University, 28200 Giresun, Turkey.
Foods. 2025 Feb 19;14(4):710. doi: 10.3390/foods14040710.
Protein-protein interactions were investigated, evaluating the influence of eggs and peanut flour on the chemical features of muffin samples. Electrophoretic, immunochemical, and chromatographic analyses were carried out to evaluate how different proteins can interact with one another, determining changes in their extractability. In this context, two extraction buffers were employed to study the rate of protein aggregate formation. Egg coagulation properties were found to affect the rate of wheat protein solubility, while the extractability of roasted peanut flour protein was less influenced and proportional to its amount in the formulation (i.e., 4% and 20%). The findings of this investigation allowed us to assume a complex form of protein organization, characterized by a "core" of wheat and egg proteins surrounded by peanut proteins, linked together through covalent reducible bonds and hydrophobic interactions. Nevertheless, the occurrence of other types of crosslinking could not be excluded.
研究了蛋白质-蛋白质相互作用,评估了鸡蛋和花生粉对松饼样品化学特性的影响。进行了电泳、免疫化学和色谱分析,以评估不同蛋白质之间如何相互作用,确定其可提取性的变化。在此背景下,使用了两种提取缓冲液来研究蛋白质聚集体的形成速率。发现鸡蛋的凝固特性会影响小麦蛋白的溶解速率,而烤花生粉蛋白的可提取性受影响较小,且与其在配方中的含量(即4%和20%)成正比。这项研究的结果使我们能够假设一种复杂的蛋白质组织形式,其特征是由小麦和鸡蛋蛋白组成的“核心”被花生蛋白包围,通过可还原的共价键和疏水相互作用连接在一起。然而,不能排除其他类型交联的存在。