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.

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.