Fabrication of enhanced aerogel template oleogels with enzyme-hydrolyzed soy protein isolate and covalent cross-linking.

In recent years, the utilization of aerogel templates in oleogels to replace animal fats has garnered considerable attention due to health concerns. This study employed a "fiber-particle core-shell nanostructure model" to combine sodium carboxymethylcellulose (CMCNa) and soy protein isolate (SPI) or SPI hydrolysate (SPIH), and freeze-dried to form aerogel template, which was then dipped into oil to induce oleogels. The results showed that adding SPIH significantly improved the physicochemical properties of oleogels. The results of ζ-potential, FTIR, and rheology demonstrated a stronger binding of SPIH to CMC-Na compared to SPI. The CMC-Na-SPIH aerogels exhibited a coarser surface and denser network structure in contrast to CMC-Na-SPI aerogels, with an oil holding capacity (OHC) of up to 84.6 % and oil absorption capacity (OAC) of 47.4 g/g. The mechanical strength of oleogels was further enhanced through chemical crosslinking. Both CMC-Na-SPI and CMC-Na-SPIH oleogels displayed excellent elasticity and reversible compressibility, with CMC-Na-SPIH oleogels demonstrating superior mechanical strength. Additionally, CMC-Na-SPIH oleogels exhibited enhanced slow release of antimicrobial substances and antioxidant properties. Increasing the content of SPI/SPIH significantly improved the mechanical strength, antioxidant capacity, and OHC of the oleogels. This research presents a straightforward and promising approach to enhance the performance of aerogel template oleogels.

Fabrication of soy protein nanoparticles based on metal-phenolic networks for stabilization of nano-emulsions delivery system.

The use of soy protein isolate (SPI) nanoparticles as a stabilizer in nano-emulsion systems has garnered significant interest. While metal-phenolic networks (MPNs) have been explored for their multifunctional surface modification capabilities, their integration with food protein-based delivery systems remains less explored. In this study, we attempt to develop a novel strategy to encapsulate cinnamaldehyde using MPNs (EGCG-Fe3+) with self-assembling soy protein nanoparticles (SE-Fe NPs) as a stabilizer for nano-emulsions. UV, Raman, and X-ray photoelectron spectroscopy analyses demonstrated that SE-Fe NPs were generated through metal-phenolic coordination and covalent interactions. SE-Fe NPs had a narrower particle size distribution and enhanced radical scavenging (up to 3.35-fold), as well as thermal stability. Furthermore, the smaller droplet size, higher modulus, higher cinnamaldehyde encapsulation efficiency (from 63.5% to 84.2%), and improved bio-accessibility of SE-Fe NPs stabilized nano-emulsions delivery system demonstrated in this study shows promising future applications in the food industry.

Development of composite electrospun films utilizing soy protein amyloid fibrils and pullulan for food packaging applications.

Electrospun films (ESF) are gaining attention for active delivery due to their biocompatibility and biodegradability. This study investigated the impact of adding soy protein amyloid fibrils (SAFs) to ESF. Functional ESF based on SAFs/pullulan were successfully fabricated, with SAFs clearly observed entangled in the electrospun fibers using fluorescence microscopy. The addition of SAFs improved the mechanical strength of the ESF threefold and increased its surface hydrophobicity from 24.8° to 49.9°. Moreover, the ESF demonstrated antibacterial properties against Escherichia coli and Staphylococcus aureus. In simulated oral disintegration tests, almost 100% of epigallocatechin gallate (EGCG) dissolved within 4 min from the ESF. In summary, the incorporation of SAFs into ESF improved their mechanical strength, hydrophobicity, and enabled them to exhibit antibacterial properties, making them promising candidates for active delivery applications in food systems. Additionally, the ESF showed efficient release of EGCG, indicating their potential for controlled release of bioactive compounds.

Quercetin directed transformation of calcium carbonate into porous calcite and their application as delivery system for future foods.

The hierarchically porous property of CaCO3 has attracted considerable attention in the field of active delivery ingredients due to its high adsorption capacity. Here, a facile and high-efficient approach to control the calcification processes of CaCO3 ending with calcite microparticles with superior porosity and stability is reported and evaluated. In this work, a series of quercetin promoted CaCO3 microparticles, using soy protein isolate (SPI) as entrapment agent, was synthesized, characterized, and their digestive behavior and antibacterial activity were evaluated. Results obtained indicated that quercetin showed good ability to direct the calcification pathway of amorphous calcium carbonate (ACC) with the formation of flower- and petal-like structures. The quercetin-loaded CaCO3 microparticles (QCM) had a macro-meso-micropore structure, which was identified to be the calcite form. The macro-meso-micropore structure provided QCM with the largest surface area of 78.984 m2g-1. The loading ratio of SPI to QCM was up to 200.94 µg per mg of QCM. The protein and quercetin composite microparticles (PQM) were produced by simply dissolving the CaCO3 core, and the obtained PQM was used for the delivery of quercetin and protein. Thermogravimetric analysis showed PQM presented with good thermal stability without the CaCO3 core. Furthermore, minor discrepancy was noted in protein conformational structures after removing the CaCO3 core. In vitro digestion revealed that approximately 80% of the loaded quercetin was released from PQM during intestinal digestion, and the released quercetin exhibited efficient transportation across the Caco-2 cell monolayer. More importantly, the PQM digesta retained enhanced antibacterial activities to inhibit growth of Escherichia coli and Staphylococcus aureus. Porous calcites show a high potential as a delivery system for food applications.

Further evaluation on structural and antioxidant capacities of soy protein isolate under multiple freeze-thaw cycles.

Multiple freeze-thaw (F-T) treatments could change a protein structure and affect its physicochemical activities. In this work, soy protein isolate (SPI) was subjected to multiple F-T treatments, and the changes in its physicochemical and functional properties were investigated. The three-dimensional fluorescence spectroscopy indicated that F-T treatments changed the structure of SPI, including an increase in surface hydrophobicity. Fourier transform infrared spectroscopy showed that SPI underwent denaturation, unfolding and aggregation due to the interchange of sulfhydryl-disulfide bonds and the exposure of hydrophobic groups. Correspondingly, the particle size of SPI increased significantly and the protein precipitation rate also increased from 16.69%/25.33% to 52.52%/55.79% after nine F-T treatments. The F-T treated SPI had a higher antioxidant capacity. Results indicate that F-T treatments may be used as a strategy to ameliorate preparation methods and improve functional characteristics of SPI, and suggest that multiple F-T treatment is an alternative way to recover soy proteins.

Structure remodeling of soy protein-derived amyloid fibrils mediated by epigallocatechin-3-gallate.

Soy protein-derived amyloid fibrils (SAFs) held desirable features, and with rational tailoring of physical structures, their techno-functions could be further improved. Here, we report a strategy for tailoring SAFs to form hydrogels with appealing mechanical properties as mediated by (-)-epigallocatechin-3-gallate (EGCG). The SAFs-EGCG complexes are characterized by measuring changes in gelling properties, identifying interfacing residues, and understanding the molecular geometry of complexes. EGCG is found to cleave rigid SAFs and induce the formation of large branched chains, which are essential for forming gel-like structures. Results in this study show that SAFs-EGCG complexes and their digesta are non-toxic in human cell lines, and these complexes are superior in inhibiting the growth of Escherichia coli and Staphylococcus aureus. This study provides new insights into remodeling structures and steering techno-functions of SAFs through interaction with EGCG, and will serve as a basis for EGCG as a potent remodeling agent of food protein-derived fibrils.

Physicochemical and oxidative stability of a soybean oleosome-based emulsion and its in vitro digestive fate as affected by (-)-epigallocatechin-3-gallate.

Oleosomes, which are pre-emulsified oil bodies found naturally in plants, have excellent stability, therefore making their use more popular in the food industries. However, the mechanism of EGCG in regulating the physicochemical and oxidative stability, and digestion of oleosome emulsions is not yet clear. In this study, the effect of EGCG on the properties of soybean oleosome emulsions (SOE) was examined at different pH values (5.0, 7.0, and 9.0). EGCG was significantly more effective in maintaining the stability of SOE at pH 5.0 and 7.0 over the 14 days of storage, but less effective at pH 9.0. Furthermore, lipid oxidation of SOE at pH 7.0 was successfully retarded by incorporating EGCG, but not at pH 5.0 and 9.0. The in vitro gastrointestinal results suggested that EGCG retarded the digestion rate of SOE based on a 20% reduction in free fatty acid release. The results of this study will help food technologists to design slow-digestive oleosome-based products that will satisfy health-conscious consumers' demand for healthier food choices.