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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. [ABSTRACT FROM AUTHOR]

Abstract: Fourier transform infrared (FTIR) method was used to study the conformations of soy protein obtained through aqueous solution and bis(2-ethylhexyl) sodium sulfosuccinate (AOT) reverse micelle extraction. The results showed that there were changes in signal intensity and/or position of IR bands at 4000–400 cm−1 when the soy proteins were separated by two extraction methods. The FTIR spectral changes were subsequently assessed using the second derivative spectroscopy in the amide I region (1700–1600 cm−1). The contents of α-helix, β-sheet, turn and irregular conformations for soy proteins using aqueous solution extraction were 11.6%, 32.8%, 44.3% and 11.3%, respectively; while using AOT reverse micelle extraction 13.1%, 41.6%, 32.5% and 12.9%, respectively. The amount change of these structures might affect functional properties of soy proteins. [Copyright &y& Elsevier]