Surface structure and volatile characteristic of peanut proteins obtained through AOT reverse micelles
Xiaoyan Zhao1, Hongkai Liu1, Xiaowei Zhang1
1Department of Food Science and Nutrition, Culinary Institute, University of Jinan, Jinan, 250022, People's Republic of China.
Abstract:
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.
Related Concept Videos
Modeling of Diode Reverse Characteristics
When a reverse voltage applied to a Zener diode exceeds its breakdown voltage, the diode enters the breakdown region. At this point, the...
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme...
Structural Protein Function
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Structural Protein Function
Volatilization
Protein and Protein Structures


