2015
DOI: 10.1007/s11746-015-2657-9
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XRD, SEM, and XPS Analysis of Soybean Protein Powders Obtained Through Extraction Involving Reverse Micelles

Abstract: 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). These analysis methods provided detailed information about elemental distributions, surface structure, and secondary and microstructures of the protein, respectively. XPS data revealed that the O and N atomic percentages of soybean protein surfaces obtained with bis(2-ethylhexyl) sodium s… Show more

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Cited by 100 publications
(58 citation statements)
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“…Their particle size distribution was also not as homogenous as the soy protein powder. Indeed, the morphology of the soy protein powders was not like those reported in Zhao et al (2015), rather than spray-dried milk protein concentrates with attached spherical shape protein on the surface (Kelly et al, 2015). The difference in these observations could be attributed to the fact that both protein concentrations and treatment procedures could have affected the morphology of protein products.…”
Section: Sem and Sem-eds Morphological Characteristicsmentioning
confidence: 88%
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“…Their particle size distribution was also not as homogenous as the soy protein powder. Indeed, the morphology of the soy protein powders was not like those reported in Zhao et al (2015), rather than spray-dried milk protein concentrates with attached spherical shape protein on the surface (Kelly et al, 2015). The difference in these observations could be attributed to the fact that both protein concentrations and treatment procedures could have affected the morphology of protein products.…”
Section: Sem and Sem-eds Morphological Characteristicsmentioning
confidence: 88%
“…There were two obvious peaks at 2θ of about 9.4 and 20⁰ in the XRD pattern of the four protein samples. These features are typical for soy protein powders, reflecting the α-helix and β-sheet structures of protein molecules, respectively (Chen et al, 2013;Luo et al, 2016;Zhao et al, 2015). The intensity of both peaks was in the order CSPa < CSPI < CSPa, indicating that the two-step fractionation unequally delivered less α-helix and β-sheet protein components into water-soluble fraction than alkali-soluble fraction.…”
Section: Xrd Examinationmentioning
confidence: 90%
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