School of Food and Biological Engineering, and Natural Food Macromolecule Research Center, Shaanxi University of Science and Technology, Xi' an 710021, China.
School of Food and Biological Engineering, and Natural Food Macromolecule Research Center, Shaanxi University of Science and Technology, Xi' an 710021, China.
Food Chem. 2021 Oct 1;358:129860. doi: 10.1016/j.foodchem.2021.129860. Epub 2021 Apr 20.
The influence of combined Lysine (Lys) and transglutaminase (TG) on the conformation and gelling properties of oxidatively damaged myofibrillar protein (MP) was investigated. The addition of Lys (5 mM) significantly increased the α-helix content (by 47.8%) and decreased the particle size of oxidatively damaged MP, and improved the cooking yield (by 16.8%) and the breaking strength of MP gels (by 65.5%). The treatment with TG (E:S = 1:500) led to a slightly reduced α-helix content but improved breaking strength (by 41.8%) and cooking loss (by 13.3%) of the gels. Their combination (Lys + TG) showed the greatest and synergistic overall improvement, with the set gel displaying a fine, smooth and compact network structure. Notably, the gelling ability of oxidatively damaged MP upon Lys + TG treatment was significantly stronger than that of non-oxidized MP far exceeding its recovery. Therefore, significantly enhanced gelling properties of oxidatively damaged MP can be attained through the combination Lys and TG.
研究了赖氨酸（Lys）和转谷氨酰胺酶（TG）联合作用对氧化损伤的肌原纤维蛋白（MP）构象和胶凝特性的影响。添加 Lys（5 mM）显著增加了氧化损伤 MP 的α-螺旋含量（增加了 47.8%），降低了颗粒大小，并提高了蒸煮得率（增加了 16.8%）和 MP 凝胶的断裂强度（增加了 65.5%）。用 TG（E：S = 1：500）处理导致α-螺旋含量略有降低，但凝胶的断裂强度（增加了 41.8%）和蒸煮损失（减少了 13.3%）得到改善。它们的组合（Lys + TG）显示出最大的协同整体改善，所得凝胶具有精细、光滑和紧凑的网络结构。值得注意的是，Lys + TG 处理后的氧化损伤 MP 的胶凝能力明显强于非氧化 MP，远远超过其恢复能力。因此，通过结合 Lys 和 TG 可以显著提高氧化损伤 MP 的胶凝特性。
