The restorative role and mechanism of L-lysine in yak myofibrillar protein gelling properties under malondialdehyde-induced over-oxidation damage
The restorative role and mechanism of L-lysine in yak myofibrillar protein gelling properties under malondialdehyde-induced over-oxidation damage
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DOI：
10.1016/j.lwt.2023.115519
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发表时间：
2023-11
期刊：
影响因子：
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通讯作者：
Hui-Qin Lu;Lin-Lin Wang-Lin;Li-Na Wang;Yi-Wen Mei;Cai-Hui Wang;Bi-Feng Xu;Na-Li
中科院分区：
文献类型：
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作者：
Hui-Qin Lu;Lin-Lin Wang-Lin;Li-Na Wang;Yi-Wen Mei;Cai-Hui Wang;Bi-Feng Xu;Na-Li
在丙二醛（MDA）氧化应激条件下，研究了不同浓度赖氨酸（L-lys、5 mmol/L、10 mmol/L、15 mmol/L和20 mmol/L）对牦牛肉肌原纤维蛋白（MP）结构和胶凝行为的影响。l -赖氨酸显著抑制了氧化引起的蛋白质结构退化，恢复了凝胶性能。固有色氨酸荧光和傅里叶变换红外光谱分析证实，l -赖氨酸的加入增强了MP的结构稳定性。从粒径和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）结果可以看出，l -赖氨酸也明显降低了氧化诱导的蛋白质交联和聚集。L-lys对MP氧化损伤的修复作用呈显著的浓度依赖性，其中在浓度为20 mmol/L时修复效果最好。这些结果表明，氧化破坏了MP的结构和凝胶特性，但l -赖氨酸有效地恢复了这些破坏性的变化。
The effects of different concentrations of L-lysine (L-lys, 5 mmol/L, 10 mmol/L, 15 mmol/L, and 20 mmol/L) on the structure and gelling behavior of yak meat myofibrillar protein (MP) under the oxidative stress of malondialdehyde (MDA) were explored. L-lys substantially inhibited the oxidation-induced structural deterioration of the proteins, and restored the gelation performance. Intrinsic tryptophan fluorescence and Fourier transform infrared spectra analysis confirmed that the addition of L-lys enhanced the structural stability of MP. L-lys also appreciably decreased oxidation-induced protein crosslinking and aggregation, as shown by particle size and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Moreover, the repair effect of L-lys on MP oxidative damage showed a significant concentration-dependent effect, in which L-lys showed the best repairment at a concentration of 20 mmol/L. These results advocate that oxidation disrupted the structure and gel characteristic of MP, but L-lys effectively restored these destructive changes.