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Surface structure and volatile characteristic of peanut proteins obtained through AOT reverse micelles
- Source :
- Colloids and Surfaces B: Biointerfaces. 173:860-868
- Publication Year :
- 2019
- Publisher :
- Elsevier BV, 2019.
-
Abstract
- 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.
- Subjects :
- Diffraction
Materials science
Arachis
Nitrogen
Surface Properties
Scanning electron microscope
Analytical chemistry
02 engineering and technology
Mass spectrometry
01 natural sciences
Micelle
Gas Chromatography-Mass Spectrometry
Mass Spectrometry
Colloid and Surface Chemistry
X-Ray Diffraction
X-ray photoelectron spectroscopy
0103 physical sciences
Surface structure
Physical and Theoretical Chemistry
Micelles
Plant Proteins
010304 chemical physics
Temperature
Water
Surfaces and Interfaces
General Medicine
021001 nanoscience & nanotechnology
Lipids
Carbon
Amorphous solid
Oxygen
Aqueous buffer
Microscopy, Electron, Scanning
0210 nano-technology
Biotechnology
Subjects
Details
- ISSN :
- 09277765
- Volume :
- 173
- Database :
- OpenAIRE
- Journal :
- Colloids and Surfaces B: Biointerfaces
- Accession number :
- edsair.doi.dedup.....a5441e15196d1c87590d1b680edaadc0
- Full Text :
- https://doi.org/10.1016/j.colsurfb.2018.10.070