Li Qian, Zhao Di, Liu Hui, Zhang Miao, Jiang Shuai, Xu Xinglian, Zhou Guanghong, Li Chunbao
Key Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
Food Chem X. 2020 Jun 10;7:100094. doi: 10.1016/j.fochx.2020.100094. eCollection 2020 Sep 30.
Myoglobin, a critical protein responsible for meat color, has been shown insusceptible to digestion. The underlying mechanism is not clear. The present study aimed to evaluate whether the structural properties of myoglobin are associated with its insusceptibility to digestion using spectroscopic and computational techniques. Myoglobin was degraded by only 7.03% by pepsin and 33.00% by pancreatin. The structure of myoglobin still maintained α-helix after the two-step digestion, with the exposure of some aromatic residues. In addition, molecular dynamics modeling suggested that hydrophobic amino acid residues (Phe 111, Leu 10, Ala 115, Pro 116) in pepsin and polar amino acid residues (Tyr 146, Thr 95) in myoglobin were found in the proximity of binding sites, which could result in the low digestibility of myoglobin. Our findings provide a new insight into the underlying mechanisms on the difficulty in digestion of myoglobin.
肌红蛋白是一种对肉色起关键作用的蛋白质，已被证明不易被消化。其潜在机制尚不清楚。本研究旨在使用光谱和计算技术评估肌红蛋白的结构特性是否与其不易消化性相关。肌红蛋白经胃蛋白酶降解仅7.03%，经胰酶降解33.00%。经过两步消化后，肌红蛋白的结构仍保持α-螺旋，一些芳香族残基暴露。此外，分子动力学建模表明，胃蛋白酶中的疏水氨基酸残基（苯丙氨酸111、亮氨酸10、丙氨酸115、脯氨酸116）和肌红蛋白中的极性氨基酸残基（酪氨酸146、苏氨酸95）位于结合位点附近，这可能导致肌红蛋白的低消化率。我们的研究结果为肌红蛋白消化困难的潜在机制提供了新的见解。
Zotero 插件
