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Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced Desolvation
Protein nanoparticles have recently found a lot of interests due to their unique physicochemical properties and structure-functionality compared to the conventional proteins. The aim of this research was to synthesize pea protein nanoparticles (PPN) using ethanol-induced desolvation, to determine th...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6669580/ https://www.ncbi.nlm.nih.gov/pubmed/31261964 http://dx.doi.org/10.3390/nano9070949 |
Sumario: | Protein nanoparticles have recently found a lot of interests due to their unique physicochemical properties and structure-functionality compared to the conventional proteins. The aim of this research was to synthesize pea protein nanoparticles (PPN) using ethanol-induced desolvation, to determine the changes in secondary structures and the particle stability in an aqueous dispersion. The nanoparticles were prepared by diluting 3.0 wt% pea protein solutions in 1–5 times ethanol at pH 3 and 10 at different temperatures. Higher ratios of ethanol caused greater extent of desolvation and larger sizes of PPN. After homogenization at 5000 psi for 5 min, PPN displayed uniform size distribution with a smaller size and higher zeta potential at pH 10 compared to pH 3. PPN prepared from a preliminary thermal treatment at 95 °C revealed a smaller size than those synthesized at 25 °C. Electron microscopy showed roughly spherical shape and extensively aggregated state of the nanoparticles. Addition of ethanol caused a reduction in β-sheets and an increase in α-helices and random coil structures of the proteins. When PPN were separated from ethanol and re-dispersed in deionized water (pH 7), they were stable over four weeks, although some solubilization of proteins leading to a loss in particle size was observed. |
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