Guo Anqi, Jiang Jiang, True Alma D, Xiong Youling L
Department of Animal and Food Sciences, University of Kentucky, Lexington, Kentucky 40546, United States.
College of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
J Agric Food Chem. 2021 Feb 3;69(4):1308-1317. doi: 10.1021/acs.jafc.0c04365. Epub 2021 Jan 25.
Protein gelation is an important phenomenon in processed meats. The present study investigated the structure-activity relationship of six phenolic compounds, that is, gallic acid (GA), chlorogenic acid (CA), propyl gallate (PG), quercetin (QT), catechin (CC), and (-)-epigallocatechin-3-gallate (EGCG) in a myofibrillar protein (MP) gelling system under controlled oxidative conditions. All phenolics induced unfolding and promoted cross-linking of MP via sulfhydryl or amine groups. At an equal molar concentration, EGCG boosted the elastic MP gel network more than other phenolics except PG. However, all three monophenols (GA, CA, and PG) and the diphenol QT increased the MP gel strength more than CC (diphenol) and EGCG (triphenol). The flavanol structure appeared to interfere with the protein gel structure development. All phenolics retarded lipid oxidation in MP-emulsion composite gels during refrigerated storage with the least polar phenolic compounds, PG and QT, showing the greatest efficacy.
蛋白质凝胶化是加工肉类中的一种重要现象。本研究在可控氧化条件下，研究了六种酚类化合物，即没食子酸（GA）、绿原酸（CA）、没食子酸丙酯（PG）、槲皮素（QT）、儿茶素（CC）和（-）-表没食子儿茶素-3-没食子酸酯（EGCG）在肌原纤维蛋白（MP）凝胶体系中的构效关系。所有酚类化合物均通过巯基或胺基诱导MP展开并促进其交联。在等摩尔浓度下，除PG外，EGCG比其他酚类化合物更能增强弹性MP凝胶网络。然而，所有三种一元酚（GA、CA和PG）和二元酚QT比CC（二元酚）和EGCG（三元酚）更能提高MP凝胶强度。黄烷醇结构似乎会干扰蛋白质凝胶结构的形成。在冷藏储存期间，所有酚类化合物均能抑制MP-乳液复合凝胶中的脂质氧化，极性最小的酚类化合物PG和QT效果最佳。
