![]() ![]() A considerable amount of water and hydrophilic substances can be solubilized in the polar cores of micelles, such as proteins and amino acids etc. The reverse micelles consist of an aqueous nano-domain facing the polar heads of the surfactant molecules, and the hydrophobic chain of the surfactants interacts with a bulk organic solvent. Reverse micelle technology is a new technology, which is a useful tool for extracting protein with good physicochemical properties like dispersibility and solubility etc. The surface composition, morphology, and physical properties of powders can affect particle–water interactions, particle–particle interactions, and particle–air interactions in food processes. However, the surface composition of protein powders is also expected to play a role in the storage, process, and/or final application, such as wetting, dispersibility, oxidative stability, flowability, and rehydration processes etc. ĭifferent treatments, including physical (such as high pressure, heat, and mild alkali), chemical (such as deamidation, phosphorylation, and acylation), and enzymatic extraction methods, could affect the structural and physicochemical properties of soybean proteins. Soybean proteins are composed of two major components, glycinin (11S globulin of about 360 kDa) and β-conglycinin (7S globulin of 180 kDa). Soybean proteins are a relatively inexpensive source of vegetable proteins, which are widely used as food ingredients owing to their high nutritional and excellent functional properties. Moreover, XRD and SEM results also showed the influence of AOT reverse micelles, which lead to more β-sheet and pore structures. The obtained results indicated that the reverse micelles could affect the C, O, and N components on the surface of soybean proteins. The O/C ratio for soybean protein obtained from AOT reverse micelles was large. ![]() The ratios of nitrogen to carbon (N/C) on the surface of soybean protein obtained through the two extraction methods were similar. XPS data revealed that the O and N atomic percentages of soybean protein surfaces obtained with bis(2-ethylhexyl) sodium sulfosuccinate (AOT)/hexane reverse micelles were higher than those obtained with aqueous buffer, whereas the percentage of atomic C was lower. These analysis methods provided detailed information about elemental distributions, surface structure, and secondary and microstructures of the protein, respectively. Soybean protein powders obtained by aqueous buffer and reverse micelle extractions were examined and characterized using X-ray photoelectron spectroscopy (XPS), X-ray diffraction (XRD), and scanning electron microscopy (SEM). ![]()
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