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In today’s food industry, the potential of bioactive compounds in preventing many chronic diseases has garnered significant attention. Many delivery systems have been developed to encapsulate these unstable bioactive compounds. Emulsion gels, as colloidal soft-solid materials, with their unique three-dimensional network structure and strong mechanical properties, are believed to provide excellent protection for bioactive substances. In the context of constructing carriers for bioactive materials, proteins are frequently employed as emulsifiers or gelling agents in emulsions or protein gels. However, in emulsion gels, when protein is used as an emulsifier to stabilize the oil/water interface, the gelling properties of proteins can also have a great influence on the functionality of the emulsion gels. Therefore, this paper aims to focus on the role of proteins’ emulsifying and gelling properties in emulsion gels, providing a comprehensive review of the formation and modification of protein-based emulsion gels to build high-quality emulsion gel systems, thereby improving the stability and bioavailability of embedded bioactive substances.

The effect of different ultrasound pretreatment powers (0–500 W) before hot air drying on the moisture migration and quality of Cantharellus cibarius (C. cibarius) was investigated in this study. The results showed that the ultrasound pretreatment accelerated the drying rate. When the ultrasound power was 400 W, the drying time of C. cibarius was reduced by 18.90% compared with the control group. The low-field nuclear magnetic resonance (LF-NMR) and magnetic resonance imaging (MRI) results showed that the ultrasound pretreatment increased the water mobility in C. cibarius. The scanning electron microscopy (SEM) results revealed that the ultrasound pretreatment promoted the expansion of intercellular pores. In addition, the rehydration capacity and quality characteristics of the ultrasound-pretreated dried C. cibarius were better than those of the control group. Overall, this study concluded that ultrasound pretreatment is a promising pretreatment method for the hot air drying of C. cibarius products to reduce the total drying time significantly and improve the retention rate of the total phenolics and flavonoids of dried C. cibarius.

The addition of food-derived antihypertensive peptides to the diet is considered a reasonable antihypertension strategy. However, data about the stability of antihypertensive peptides in different food processing conditions are limited. In this study, through Sephadex G-15 gel chromatography and RP-HPLC separation, UPLC–ESI–MS/MS analysis and in silico screening, two novel ACE-inhibitory peptides, Pro-Leu-Leu-Lys (IC50: 549.87 μmol/L) and Pro-Pro-Met-Trp-Pro-Phe-Val (IC50: 364.62 μmol/L), were identified in millet bran glutelin-2 hydrolysates. The inhibition of angiotensin-I converting enzyme and the potential safety of PLLK and PPMWPFV were studied using molecular docking and in silico prediction, respectively. The results demonstrated that PLLK and PPMWPFV could non-competitively bind to one and seven binding sites of ACE through short hydrogen bonds, respectively. Both PLLK and PPMWPFV were resistant to different pH values (2.0–10.0), pasteurization conditions, addition of Na+, Mg2+ or K+ and simulated gastrointestinal digestion. However, PLLK and PPMWPFV were unstable upon heat treatment at 100 °C for more than 20 min or treatment with Fe3+ or Zn2+. In fact, treatment with Fe3+ or Zn2+ induced the formation of PLLK–iron or PLLK–zinc chelates and reduced the ACE-inhibitory activity of PLLK. These results indicate that peptides derived from millet bran could be added to foods as antihypertension agents.

In this study, a calcium-binding peptide was obtained by hydrolyzing tilapia bone and its osteogenic activity was evaluated. Animal protease was selected from nine enzymes, and its hydrolysate was purified through preparative and semi-preparative reverse phase high-performance liquid chromatography. The purified peptide was identified as DGPSGPK (656.32 Da) and its calcium-binding capacity reached 111.98 µg/mg. The peptide calcium chelate (DGPSGPK-Ca) was obtained, and its structure was characterized through Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), scanning electron microscopy (SEM), and mass spectrometry (MS). The results of XRD and SEM showed that DGPSGPK-Ca was formed as a new compound. The carboxyl and amino groups of Lys and Asp residues may be the chelating sites of DGPSGPK according to the FTIR and MS results. The molecular simulation showed the carbonyl groups of Asp, Pro, Ser, and Lys residues involved in the binding of calcium. The interaction of DGPSGPK and different integrins was evaluated by molecular docking simulation, and the main forces involved were electrostatic interaction forces, hydrogen bonding and hydrophobic interactions. Furthermore, DGPSGPK could inhibit the differentiation of osteoclast and promote the proliferation, differentiation and mineralization of osteoblasts.