pH 值对猪肌原纤维蛋白与吡嗪类化合物相互作用的影响。
Effect of pH on the interaction of porcine myofibrillar proteins with pyrazine compounds.
机构信息
School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China.
School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China; Overseas Expertise Introduction Center for Discipline Innovation of Food Nutrition and Human Health (111 Center), Guangzhou 510641, China.
出版信息
Food Chem. 2019 Jul 30;287:93-99. doi: 10.1016/j.foodchem.2019.02.060. Epub 2019 Feb 21.
The influence of pH-induced structural modifications of myofibrillar proteins (MPs) on their interaction mechanisms with pyrazine compounds was investigated. At a lower pH (4.9, 5.5), MPs aggregated to larger particle sizes due to enhanced the protein-protein interactions. The binding with pyrazine compounds was strongly affected by pH and the nature of flavor compounds. MPs exhibited flavor releasing behavior, probably due to protein-protein interactions and surface tension. Fluorescence analysis revealed that the interaction of pyrazine compounds with MPs followed a combination of static and dynamic quenching. The changes in quenching constant (K) might be attributed to a dynamic quenching, probably due to protein aggregation. The percentages of free 2,5-Dimethylpyrazine (2,5-DMP) were similar to K. Thermodynamic parameters indicated that electrostatic interactions and hydrophobic interactions were the major acting forces in the binding of MPs to 2,5-DMP. The binding of 2,5-DMP increased the α-helix content of MPs.
研究了肌原纤维蛋白 (MPs) 的 pH 诱导结构修饰对其与吡嗪类化合物相互作用机制的影响。在较低的 pH（4.9、5.5）下，由于蛋白质-蛋白质相互作用增强，MPs 聚集到更大的颗粒尺寸。与吡嗪类化合物的结合受 pH 和风味化合物性质的强烈影响。MPs 表现出释放风味的行为，可能是由于蛋白质-蛋白质相互作用和表面张力。荧光分析表明，吡嗪类化合物与 MPs 的相互作用遵循静态和动态猝灭的组合。猝灭常数 (K) 的变化可能归因于动态猝灭，可能是由于蛋白质聚集。游离 2,5-二甲基吡嗪（2,5-DMP）的百分比与 K 相似。热力学参数表明，静电相互作用和疏水相互作用是 MPs 与 2,5-DMP 结合的主要作用力。2,5-DMP 的结合增加了 MPs 的α-螺旋含量。
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