Department of Physics, Science of College, Nanjing Agricultural University, Nanjing 210095, PR China.
Department of Applied Mathematics, Science of College, Nanjing Agricultural University, Nanjing 210095, PR China.
Int J Biol Macromol. 2014 Mar;64:162-7. doi: 10.1016/j.ijbiomac.2013.12.003. Epub 2013 Dec 8.
β-Lactoglobulin (β-LG) is the major constituent of whey food, which has been shown to interact with a wide range of aroma compounds. In the present work, a model aroma compound, β-ionone, is used to investigate the influence of aroma compounds on the urea-induced unfolding of β-LG at pH 7.0. β-Ionone is observed to enhance the stability of β-LG at pH 7.0. Moreover, the amyloid fibrils are observed when β-LG at pH 7.0 is incubated for 12-20 days at 37 °C in the presence of 3-5M urea. However, the formation of amyloid fibrils is inhibited when β-ionone is added into the samples and the inhibitory effects follow a concentration-dependent fashion. There is a clear correlation between Cm and lag time. The correlation demonstrates that protein stability affects the amyloid fibril formation of β-LG. The results highlight the critical role of protein stability and provide an approach to prevent the formation of amyloid fibrils in vitro.
β-乳球蛋白（β-LG）是乳清食品的主要成分，已被证明能与广泛的香气化合物相互作用。在本工作中，使用模型香气化合物β-紫罗兰酮来研究香气化合物对 pH 值为 7.0 时β-LG 脲诱导展开的影响。β-紫罗兰酮被观察到能增强β-LG 在 pH 值为 7.0 时的稳定性。此外，当β-LG 在 pH 值为 7.0 时在 37°C 下在 3-5M 脲存在下孵育 12-20 天时，观察到淀粉样纤维的形成。然而，当将β-紫罗兰酮加入到样品中时，淀粉样纤维的形成被抑制，并且抑制作用呈浓度依赖性。Cm 和滞后时间之间存在明显的相关性。该相关性表明蛋白质稳定性影响β-LG 的淀粉样纤维形成。结果突出了蛋白质稳定性的关键作用，并提供了一种防止体外淀粉样纤维形成的方法。
