In this study, Tiger nut (Cyperus esculentus L.) oil-based oleogels were prepared using the emulsion template method with whey protein (WPI; 0.5–2.5% (w/v) and Xanthan gum (XG; 0.1–0.5% (w/v). The microstructure of the oleogels obtained from the high internal phase emulsion (HIPE) and an emulsion after further shearing were observed using an optical microscope and laser confocal microscopy. A series of rheological tests were conducted to evaluate the effect of WPI and XG concentrations on the strength of the emulsion and oleogel. The texture, oil holding capacity, and oxidative stability of oleogels were characterized. The results showed that XG alone could not form oleogel, while the concentration of WPI had more effect than XG. When WPI was at a fixed concentration, the viscoelasticity of HIPE increased with the addition of XG. This was due to the complexation of WPI and XG, forming a stable gel network between the tight emulsion droplets and thus giving it a higher viscoelasticity. With an increase in WPI concentration, the stability and viscoelasticity of the emulsion were increased, and the oil-holding capacity and gel strength of the oleogels were enhanced. Moreover, the addition of XG could significantly enhance the stability and viscoelasticity of the emulsion (p < 0.05), and an increase in the concentration had a positive effect on it. The oleogels showed high gel strength (G′ > 15,000 Pa) and good thixotropic recovery when the XG concentration was higher than 0.3% (w/v). WPI (2.0%) and XG (>0.3%) could be used to obtain HIPE with good physicochemical and viscoelastic properties, which in turn lead to oleogels with minimal oil loss, viscoelastic and thixotropic recovery, and temperature stability. Compared with tiger nut oil-based oleogel, tiger nut oil contained more polyunsaturated fatty acids, which were more easily decomposed through oxidation during storage and had lower oxidation stability. This study provides a reference for the preparation of oleogels from food-approved polymers and provides additional theoretical support for their potential application as solid fat substitutes.

In this study, we have investigated the effects of Tremella fuciformis polysaccharide (TP) on the pasting, rheological, structural and in vitro digestive properties of Cyperus esculentus starch (CS). The results showed that the addition of TP significantly changed the pasting characteristics of CS, increased the pasting temperature and pasting viscosity, inhibited pasting, reduced the exudation of straight-chain starch and was positively correlated with the amount of TP added. The addition of the appropriate amount of TP could increase its apparent viscosity and enhance its viscoelasticity. The composite system of CS/TP exhibited higher short-range ordered structure and solid dense structure, which protected the crystal structure of CS, but was related to the amount of TP added. In addition, the introduction of TP not only decreased the in vitro digestion rate of CS and increased the content of slow-digestible starch (SDS) and resistant starch (RS), but also reduced the degree of digestion. Correlation studies established that TP could improve the viscoelasticity, relative crystallinity and short-range order of the CS/TP composite gel, maintain the integrity of the starch granule and crystalline structure, reduce the degree of starch pasting and strengthen the gel network structure of CS, which could help to lower the digestibility of CS.

Using a multidisciplinary approach, this paper was designed to prepare, identify, and characterize novel maize antioxidant cyclic peptides from protein hydrolysate of corn gluten meal (CGM). A bioinformatics approach was used to identify the best protease, and the results showed that papain+subtilisin was most likely to produce antioxidant cyclic peptides. The result of the enzymatic hydrolysis validation experiment showed that hydrolysate by papain+subtilisin yielded the highest concentration of cyclic peptide (67.14 ± 1.88%) and remarkable DPPH, ABTS, and hydroxyl radical scavenging rates (81.06 ± 2.23%, 82.82 ± 1.83%, and 47.44 ± 2.43%, respectively) compared to other hydrolysates. Eleven antioxidant cyclic peptides were identified in the protein hydrolysate of CGM through sequential purification and mass spectrometry analysis. The results of molecular docking analysis indicated that the cyclic peptides can form stable hydrogen bonds and hydrophobic interactions with the key amino acid residues of Kelch-like ECH-associated protein 1 (Keap1). Cyclic peptides may regulate the Keap1-Nrf2 pathway by occupying the Kelch domain of Keap1, inhibiting the ubiquitination degradation of Nrf2 (nuclear factor erythroid 2-related factor 2), thereby stabilizing the Nrf2 protein and activating the antioxidant gene network. This study underlined the bioinformatics approach for antioxidant cyclic peptide discovery, which is time- and cost-effective and promotes new cyclic peptide drugs or functional food development.