Surface structure and volatile characteristic of peanut proteins obtained through AOT reverse micelles

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.Graphical abstract
Source: Colloids and Surfaces B: Biointerfaces - Category: Biochemistry Source Type: research