Department of Biotechnology, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
Exploratory Research Center on Life andLiving Systems, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi 444-8787, Japan.
J Agric Food Chem. 2024 Apr 17;72(15):8774-8783. doi: 10.1021/acs.jafc.3c09357. Epub 2024 Apr 8.
Proteins can be adsorbed on the air-water interface (AWI), and the structural changes in proteins at the AWI are closely related to the foaming properties of foods and beverages. However, how these structural changes in proteins at the AWI occur is not well understood. We developed a method for the structural assessment of proteins in the foam state using hydrogen/deuterium exchange mass spectrometry. Adsorption sites and structural changes in human serum albumin (HSA) were identified in situ at the peptide-level resolution. The -terminus and the loop (E492-T506), which contains hydrophobic amino acids, were identified as adsorption sites. Both the structural flexibility and hydrophobicity were considered to be critical factors for the adsorption of HSA at the AWI. Structural changes in HSA were observed after more than one minute of foaming and were spread widely throughout the structure. These structural changes at the foam AWI were reversible.
蛋白质可以吸附在气液界面（AWI）上，蛋白质在 AWI 上的结构变化与食品和饮料的发泡性能密切相关。然而，蛋白质在 AWI 上的这些结构变化是如何发生的还不是很清楚。我们开发了一种使用氢/氘交换质谱法对泡沫状态下蛋白质进行结构评估的方法。在原位以肽级分辨率鉴定了人血清白蛋白（HSA）的吸附位点和结构变化。-末端和环（E492-T506），其中包含疏水性氨基酸，被鉴定为吸附位点。结构的灵活性和疏水性都被认为是 HSA 在 AWI 上吸附的关键因素。在发泡一分钟以上后观察到 HSA 的结构变化，并广泛分布在整个结构中。泡沫 AWI 处的这些结构变化是可逆的。
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