Food emulsifier based on the interaction of casein and butyrylated dextrin for improving stability and emulsifying properties.

Green hydrophobically modified butyrylated dextrin (BD) was used to modulate casein (CN). The CN/BD complex nanoparticles were formed at different CN-to-BD mass ratios based on a pH-driven technology. The interaction force, stability, and emulsifying properties of complex nanoparticles were investigated. The nanoparticles had a negative charge and a small particle size (160.03, 152.6, 155.9, 206.13, and 231.67 nm) as well as excellent thermal stability and environmental stability (pH 4.5, 5.5, 6.6, 7.5, 8.5, and 9.5; ionic strength, 50, 100, 200, and 500 mM). Transmission electron microscopy demonstrated the successful preparation of complex nanoparticles and their spherical shape. Fourier transform infrared spectroscopy, fluorescence spectroscopy, and dissociation analysis results showed that the main driving forces of formed CN/BD nanoparticles were hydrogen bonding and hydrophobic interaction. Furthermore, the CN/BD nanoparticles (CN/BD mass ratio, 1:1; weight/weight) exhibited the lowest creaming index, and optical microscopy showed that it has the most evenly dispersed droplets after 7 d of storage, which indicates that the CN/BD nanoparticles had excellent emulsifying properties. Butyrylated dextrin forms complex nanoparticles with CN through hydrogen bonding and hydrophobic interaction to endow CN with superior properties. The results showed that it is possible to use pH-driven technology to form protein-polysaccharide complex nanoparticles, which provides some information on the development of novel food emulsifiers based on protein-polysaccharide nanoparticles. The study provided significant information on the improvement of CN properties and the development of emulsions based on CN.

Oligopeptides from Jinhua ham prevent alcohol-induced liver damage by regulating intestinal homeostasis and oxidative stress in mice.

The current study aimed to evaluate the protective activity of peptides isolated from Jinhua ham (JHP) against alcoholic liver disease (ALD) and the mechanisms by which JHP prevents against ALD. The tangential flow filtration (TFF) combined with size exclusion chromatography (SEC) and reversed-phase high performance liquid chromatography (RP-HPLC) were used to isolate the JHP. Then the hepatoprotective activity of peptides was evaluated through experiments in mice. The primary structure of the peptide with the strongest liver protective activity was Lys-Arg-Gln-Lys-Tyr-Asp (KRQKYD) and the peptide was derived from the myosin of Jinhua ham, which were both identified by LC-MS/MS. Furthermore, the mechanism of KRQKYD prevention against ALD was attributed to the fact that KRQKYD increases the abundance of Akkermansia muciniphila in the gut and decreases the abundance of Proteobacteria (especially Escherichia_Shigella). The LPS-mediated liver inflammatory cascade was reduced by protecting the intestinal barrier, increasing the tight connection of intestinal epithelial cells and reducing the level of LPS in the portal venous circulation. KRQKYD could inhibit the production of ROS by upregulating the expression of the NRF2/HO-1 antioxidant defense system and by reducing oxidative stress injury in liver cells. This study can provide a theoretical foundation for the application of JHP in the protection of liver from ALD.