Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced Desolvation

Abstract

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.

Prediction of emulsification behaviour of pea and faba bean protein concentrates and isolates from structure–functionality analysis

“…Bovine serum albumin (BSA) was used as an internal standard for the protein content determination from the absorbance. 27 The protein solubility (% S ) was calculated by eqn (1) . …”

Biophysical and Structural Insights in α‐Amylase and Bile Acids interaction

“…TDCA caused a significant increase in β‐sheet structure at expense of α‐helix loss structure, being this effect more evident at higher concentration of TDCA. These findings could be due to the increase in negative charge that promotes the hydrogen bond in β‐sheet structures [17] . On the second derivative curve, a gradual decrease in the contribution of the unordered structure and an increase in the contribution of the β‐sheet intensity peak was observed.…”

“…These findings could be due to the increase in negative charge that promotes the hydrogen bond in β-sheet structures. [17] On the second derivative curve, a gradual decrease in the contribution of the unordered structure and an increase in the contribution of the β-sheet intensity peak was observed. The second derivative spectra corresponding to each situation mentioned above are shown in Supplementary Fig- ure S1.…”

Biopolymer nanoparticles: a strategy to enhance stability, bioavailability, and biological effects of phenolic compounds as functional ingredients

“…Once the polymer–polymer interactions overcome polymer–solvent interactions, nucleation of polymer particles begins, followed by nuclei aggregation and nanoparticle formation. It stops when the polymer concentration dissolved is below the critical supersaturation concentration 79 . In other words, there are three main steps in nanoparticle formation by desolvation: (i) supersaturation; (ii) nucleation; and (iii) expansion of nuclei 66 .…”

“…It stops when the polymer concentration dissolved is below the critical supersaturation concentration. 79 In other words, there are three main steps in nanoparticle formation by desolvation: (i) supersaturation; (ii) nucleation; and (iii) expansion of nuclei. 66 In addition, later stabilization of nanoparticles can be done by chemical crosslinking.…”