Ethanol as a switch to induce soybean lipophilic protein self-assembly and resveratrol delivery.

Protein-based nanoparticles or nanocarriers of emulsion systems have piqued the interest of nutrition and health care goods. As a result, this work examines the characterisation of ethanol-induced soybean lipophilic protein (LP) self-assembly for resveratrol (Res) encapsulation, particularly the influence on emulsification. By varying the ethanol content ([E]) in the range of 0-70% (v/v), the structure, size, and morphology of LP nanoparticles may be adjusted. Similarly, the self-assembled LPs have a strong [E] dependency on the encapsulation efficiency of Res. For [E] = 40% (v/v), Res had the highest encapsulation efficiency (EE) and load capacity (LC) of 97.1% and 141.0 µg/mg nanoparticles, respectively. Most of the Res was encapsulated by the hydrophobic core of LP. Moreover, for [E] = 40% (v/v), LP-Res showed significantly improved emulsifying properties, independent of low-oil or high-oil emulsion systems. Furthermore, the ethanol-induced production of appropriate aggregates increased emulsion system stability, hence increasing Res retention during storage.

Ultrasound-assisted alkali removal of proteins from wastewater generated during oil bodies extraction.

In this study, an ultrasonic-assisted alkaline method was used to remove proteins from wastewater generated during oil-body extraction, and the effects of different ultrasonic power settings (0, 150, 300, and 450 W) on protein recovery were investigated. The recoveries of the ultrasonically treated samples were higher than those of the samples without ultrasonic treatment, and the protein recoveries increased with increasing power, with a protein recovery of 50.10 % ± 0.19 % when the ultrasonic power was 450 W. Amino acid analysis showed that the amino acids comprising the recovered samples were consistent, regardless of the ultrasonic power used, but significant differences in the contents of amino acids were observed. No significant changes were observed in the protein electrophoretic profile using dodecyl polyacrylamide gel, indicating that sonication did not change the primary structures of the recovered samples. Fourier transform infrared and fluorescence spectroscopy revealed that the molecular structures of the samples changed after sonication, and the fluorescence intensity increased gradually with increasing sonication power. The contents of α-helices and random coils obtained at an ultrasonic power of 450 W decreased to 13.44 % and 14.31 %, respectively, whereas the ß-sheet content generally increased. The denaturation temperatures of the proteins were determined using differential scanning calorimetry, and ultrasound treatment reduced the denaturation temperatures of the samples, which was associated with the structural and conformational changes caused by their chemical bonding. The solubility of the recovered protein increased with increasing ultrasound power, and a high solubility was essential in good emulsification. The emulsification of the samples was improved well. In conclusion, ultrasound treatment changed the structure and thus improved the functional properties of the protein.

Dithiothreitol-induced reassembly of soybean lipophilic protein as a carrier for resveratrol: Preparation, structural characterization, and functional properties.

We employed dithiothreitol (DTT) to reassemble soy lipophilic protein (LP) and increased its solubility for encapsulating resveratrol (Res); we subsequently added hydroxypropyl methylcellulose (HPMC) to further stabilize Res. Physicochemical characterization, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and spectral analysis revealed that DTT triggered the breakage and reassembly of the disulfide bond. Consequently, the solubility of LP increased from 38.64 % to 71.49 %, and the number of free sulfhydryl groups increased to 7.84 mol·g-1. Furthermore, the encapsulation efficiency and structure of reassembled LP nanoparticles loaded with Res were found to be closely related to the DTT concentration used for induction. When HPMC was added, the LP-Res complex demonstrated spontaneous self-assembly, and the pH and temperature stability of the Res in the nanoparticles improved. An in vitro digestion simulation revealed that the reassembled LP was an efficient carrier for Res delivery. Particularly, HPMC improved the bioavailability and sustained release of Res.

Sodium Dodecyl Sulfate-Dependent Disassembly and Reassembly of Soybean Lipophilic Protein Nanoparticles: An Environmentally Friendly Nanocarrier for Resveratrol.

The development of protein-based nanocarriers to improve the water solubility, stability, and bioavailability of hydrophobic or poorly soluble bioactive molecules has attracted increasing interest in the food and pharmaceutical industries. In this study, a network-like nanostructure of soybean lipophilic protein (LP) was obtained through sodium dodecyl sulfate (SDS)-dependent decomposition and recombination. This nanostructure served as an excellent nanocarrier for resveratrol (Res), a poorly soluble biologically active molecule. The structure of LP gradually decomposed into its independent subunits at SDS concentrations ≤5% (w/v). After the removal of SDS, the dissociated subunits partially reassembled into a fibrous network-like nanostructure in which the Res molecules were encapsulated, and they preferentially interacted with the hydrophobic subunits (α and α' subunits and the 24 kDa subunit) of the protein. This system exhibited a high encapsulation efficiency (95.93%), high water solubility (85.29%), extraordinary oxidation resistance (DPPH radical scavenging activity of 67.1%), and improved Res digestibility (78.7%).