Department of Food Science and Nutrition, Culinary Institute, University of Jinan, Jinan, 250022, People's Republic of China.
Department of Food Science and Nutrition, Culinary Institute, University of Jinan, Jinan, 250022, People's Republic of China.
Colloids Surf B Biointerfaces. 2019 Jan 1;173:860-868. doi: 10.1016/j.colsurfb.2018.10.070. Epub 2018 Oct 25.
This study provided the investigation of the surface structure and volatile compounds of peanut proteins obtained through aqueous buffer (AB) and reverse micelles (RMs) by X-ray diffraction (XRD), scanning electron microscopy (SEM), X-ray photoelectron spectroscopy (XPS) and gas chromatography-mass spectrometry (GC-MS). The results showed that RMs could modify the amorphous structure of peanut proteins and change the original structure. Significant differences were between the C, O, and N content in two type protein surfaces (P < 0.05).The O/C ratio from AB was higher than from RMs, but the N/C ratio was lower. These changes suggested that RMs could modify the surface morphology and composition of peanut proteins. Untargeted profiling of volatile compounds showed that the volatile compounds of peanut proteins obtained by AB and RMs were major differences. Such finding suggested that RMs could contribute to improve the flavor properties of peanut protein.
本研究通过 X 射线衍射（XRD）、扫描电子显微镜（SEM）、X 射线光电子能谱（XPS）和气相色谱-质谱联用（GC-MS），对水缓冲液（AB）和反胶束（RMs）提取的花生蛋白的表面结构和挥发性化合物进行了研究。结果表明，RMs 可以改变花生蛋白的无定形结构，使原始结构发生显著变化。两种类型蛋白质表面的 C、O 和 N 含量存在显著差异（P<0.05）。AB 提取的蛋白质表面 O/C 比值高于 RMs 提取的，而 N/C 比值则较低。这些变化表明，RMs 可以改变花生蛋白的表面形态和组成。非靶向挥发性化合物分析表明，AB 和 RMs 提取的花生蛋白的挥发性化合物存在显著差异。这一发现表明，RMs 可以改善花生蛋白的风味特性。
