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...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2019-06-01
|
| Series: | Nanomaterials |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2079-4991/9/7/949 |
| _version_ | 1811334982593937408 |
|---|---|
| author | Chi Diem Doan Supratim Ghosh |
| author_facet | Chi Diem Doan Supratim Ghosh |
| author_sort | Chi Diem Doan |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-13T17:17:13Z |
| format | Article |
| id | doaj.art-0899f91a9297410bb2e5fd7acc893e39 |
| institution | Directory Open Access Journal |
| issn | 2079-4991 |
| language | English |
| last_indexed | 2024-04-13T17:17:13Z |
| publishDate | 2019-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Nanomaterials |
| spelling | doaj.art-0899f91a9297410bb2e5fd7acc893e392022-12-22T02:38:06ZengMDPI AGNanomaterials2079-49912019-06-019794910.3390/nano9070949nano9070949Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced DesolvationChi Diem Doan0Supratim Ghosh1Laboratory of Food Nanotechnology, Department of Food and Bioproduct Sciences, College of Agriculture and Bioresources, University of Saskatchewan, Saskatoon, SK S7N 5A8, CanadaLaboratory of Food Nanotechnology, Department of Food and Bioproduct Sciences, College of Agriculture and Bioresources, University of Saskatchewan, Saskatoon, SK S7N 5A8, CanadaProtein 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.https://www.mdpi.com/2079-4991/9/7/949pea proteinalcohol-desolvationnanoparticlessecondary structuredispersion stabilityaccelerated gravitation |
| spellingShingle | Chi Diem Doan Supratim Ghosh Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced Desolvation Nanomaterials pea protein alcohol-desolvation nanoparticles secondary structure dispersion stability accelerated gravitation |
| title | Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced Desolvation |
| title_full | Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced Desolvation |
| title_fullStr | Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced Desolvation |
| title_full_unstemmed | Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced Desolvation |
| title_short | Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced Desolvation |
| title_sort | formation and stability of pea proteins nanoparticles using ethanol induced desolvation |
| topic | pea protein alcohol-desolvation nanoparticles secondary structure dispersion stability accelerated gravitation |
| url | https://www.mdpi.com/2079-4991/9/7/949 |
| work_keys_str_mv | AT chidiemdoan formationandstabilityofpeaproteinsnanoparticlesusingethanolinduceddesolvation AT supratimghosh formationandstabilityofpeaproteinsnanoparticlesusingethanolinduceddesolvation |