Effect of reverse micelle on conformation of soy globulins: A Raman study

Zhao, Xiaoyan; Ao, Qiang; Chen, Fusheng; Xue, Wei; Li-te, LI; Liu, Jie

doi:10.1016/j.foodchem.2009.02.028

Cited by 16 publications

(16 citation statements)

References 27 publications

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“…These results indicated that there was little difference in the percentage of α‐helix and β‐sheet structures from the 11S globulin using the two extraction methods. These results agreed with the investigation by Zhao et al …”

Section: Resultssupporting

confidence: 94%

“…However, the intensity of the 7S globulin using reverse micelle extraction at 2 θ about 22° slightly increased compared with the intensity of the 7S globulin reflection using aqueous buffer extraction. The result suggested that the environment of AOT reverse micelles had no effect on the percentage of the β‐sheet of the 7S globulin . The characteristic reflections of 11S globulin using AOT reverse micelle extraction at 2 θ about 10 and 22° had slightly decreased intensities, showing that the presence of AOT reverse micelle did not reduce the crystallinity of the 11S globulin.…”

Section: Resultsmentioning

confidence: 95%

“…The intensities of the 7S globulin using two extraction methods at 2 θ about 10° were 83.2% and 73.4%, respectively, which were significantly different ( P < 0.05) (Table ). It indicated that the percentage of α‐helix structure of the 7S globulin using AOT reverse micelles decreased . This phenomenon occurred through insertion of AOT reverse micelles into the crystalline structure, thus modifying the microstructure of the 7S globulin.…”

Section: Resultsmentioning

confidence: 98%

“…( W 0 ) = 18 in isooctane at room temperature], and co‐surfactants are not necessary . The secondary structures and functional properties of 7S and 11S globulins using AOT reverse micelle extraction have been extensively investigated . More recently, Zhao and co‐workers demonstrated by Fourier transform infrared (FTIR) that an AOT reverse micelle system could modify the secondary structure in amides I of the 7S and 11S globulins.…”

Section: Introductionmentioning

confidence: 99%

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Determination of the domain structure of the 7S and 11S globulins from soy proteins by XRD and FTIR

et al. 2012

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Section: Resultssupporting

confidence: 94%

Section: Resultsmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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Determination of the domain structure of the 7S and 11S globulins from soy proteins by XRD and FTIR

et al. 2012

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“…The results indicated that AOT reverse micelles could purify the walnut protein. This fact also suggested that the reverse micelles might change the original structure of walnut protein surface, which could have a significant impact on physical–chemical properties of walnut protein (Zhao et al ., , ).…”

Section: Resultsmentioning

confidence: 99%

Surface properties of walnut protein from AOT reverse micelles

Liu

Wang

Zhao

et al. 2013

Int J of Food Sci Tech

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Summary The surface chemical composition and microstructure of walnut protein obtained through aqueous buffer and bis(2‐ethylhexyl) sodium sulfosuccinate (AOT) reverse micelles were determined by X‐ray photoelectron spectroscopy (XPS) and scanning electron microscopy (SEM). The surfaces were characterised by XPS to monitor surface composition. The different components of C 1s, N 1s and O 1s peaks were provided precisely. By comparison with walnut protein surface from aqueous buffer, XPS analysis revealed that the O atomic percentage of walnut protein powder surface from AOT reverse micelles was higher, but the C and N atomic percentages were lower. The N/C ratio of the walnut protein powders using two extraction methods was similar, while significant difference was obtained in the O/N. The obtained results indicated that the reverse micelles could affect the C, O and N components on the surface of walnut protein powder. Protein microstructure after reverse micelle treatment showed many crystals.

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XRD, SEM, and XPS Analysis of Soybean Protein Powders Obtained Through Extraction Involving Reverse Micelles

Zhao

Zhu

Zhang

et al. 2015

J Americ Oil Chem Soc

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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 sulfosuccinate (AOT)/hexane reverse micelles were higher than those obtained with aqueous buffer, whereas the percentage of atomic C was lower. The ratios of nitrogen to carbon (N/C) on the surface of soybean protein obtained through the two extraction methods were similar. The O/C ratio for soybean protein obtained from AOT reverse micelles was large. The obtained results indicated that the reverse micelles could affect the C, O, and N components on the surface of soybean proteins. Moreover, XRD and SEM results also showed the influence of AOT reverse micelles, which lead to more β-sheet and pore structures.

show abstract

Effect of reverse micelle on conformation of soy globulins: A Raman study

Cited by 16 publications

References 27 publications

Determination of the domain structure of the 7S and 11S globulins from soy proteins by XRD and FTIR

Determination of the domain structure of the 7S and 11S globulins from soy proteins by XRD and FTIR

Surface properties of walnut protein from AOT reverse micelles

XRD, SEM, and XPS Analysis of Soybean Protein Powders Obtained Through Extraction Involving Reverse Micelles

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