Oil-in-water and oleogel-in-water emulsion encapsulate with hemp seed oil containing Δ9-tetrahydrocannabinol and cannabinol: Stability, degradation and in vitro simulation characteristics.

The present study focused on investigating the stability and in vitro simulation characteristics of oil-in-water (O/W) and oleogel-in-water (Og/W) emulsions. Compared with O/W emulsion, the Og/W emulsion exhibited superior stability, with a more evenly spread droplet distribution, and the Og/W emulsion containing 3 % hemp seed protein (HSP) showed better stability against environmental factors, including heat treatment, ionic strength, and changes in pH. Additionally, the stability of Δ9-tetrahydrocannabinol (Δ9-THC) and cannabinol (CBN) and the in vitro digestion of hemp seed oil (HSO) were evaluated. The half-life of CBN in the Og/W emulsion was found to be 131.82 days, with a degradation rate of 0.00527. The in vitro simulation results indicated that the Og/W emulsion effectively delayed the intestinal digestion of HSO, and the bioaccessibility of Δ9-THC and CBN reached 56.0 % and 58.0 %, respectively. The study findings demonstrated that the Og/W emulsion constructed with oleogel and HSP, exhibited excellent stability.

Effect of dynamic high-pressure microfluidization treatment on soybean protein isolate-rutin non-covalent complexes.

In this investigation, soybean protein isolate-rutin (SPI-RT) complexes were treated using dynamic high-pressure microfluidization (DHPM). The effects of this process on the physicochemical and thermodynamic properties of SPI were investigated at different pressures. Fourier-transform infrared spectroscopy and fluorescence spectroscopy provided evidence that the SPI structure had been altered. The binding of SPI to RT resulted in a decrease in the percentage of α-helices and random curls as well as an increase in the percentage of ß-sheets. In particular, the α-helix content decreased from 29.84 % to 26.46 %, the random curl content decreased from 17.45 % to 15.57 %, and the ß-sheet content increased from 25.37 % to 26.53 %. Moreover, fluorescence intensity decreased, and the emission peak of the complex was red-shifted by 6 nm, exposing the internal groups. Based on fluorescence quenching analysis, optimal SPI-RT complexation was achieved after 120-MPa DHPM treatment, and molecular docking analysis verified the interaction between SPI and RT. The minimum particle size, maximum absolute potential, and total phenolic content of the complexes were 78.06 nm, 21.4 mV and 74.35 nmol/mg protein, respectively. Furthermore, laser confocal microscopy revealed that the complex particles had the best microstructure. Non-covalent interactions between the two were confirmed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Moreover, the hydrophobicity of the complex particle's surface increased to 16,045 after 120-MPa DHPM treatment. The results of this study suggest that DHPM strongly promotes the improvement of the physicochemical properties of SPI, and provide a theoretical groundwork for further research.

Ultrasonic treatment of rice bran protein-tannic acid stabilized oil-in-water emulsions: Focus on microstructure, rheological properties and emulsion stability.

Rice bran protein (RBP)-tannic acid (TA) complex was prepared and the RBP-TA emulsions were subjected to ultrasonic treatment with different powers. Ultrasonic treatment has a positive effect on improving the properties of RBP-TA emulsion. This study investigated the influence of different ultrasonic power levels on the physicochemical properties, microstructure, rheological properties, and stability of emulsions containing RBP-TA. Under the ultrasonic treatment of 400 W, the particle size, zeta potential, and adsorbed protein content of the RBP-TA emulsion were 146.86 nm, -20.7 eV, and 61.91%, respectively. At this time, the emulsion had the best emulsifying properties, apparent viscosity, energy storage modulus and loss modulus. In addition, the POV and TBARS values of RBP-TA emulsions were 6.12 and 7.60 mmol/kg, respectively. The thermal, salt ion, pH and oxidative stability of the emulsions were investigated, and it was shown that ultrasonic treatment was effective in improving the stability of RBP-TA emulsions.

Covalent binding of ultrasound-treated japonica rice bran protein to catechin: Structural and functional properties of the complex.

Due to the existence of many disulfide bonds in japonica rice bran protein (JRBP) molecules, their solubility is poor, which seriously affects other functional properties. To improve the functional characteristics of JRBP molecules, they were processed by ultrasound technology, and JRBP-catechin (CC) covalent complex was prepared. The structural and functional properties of indica and japonica rice bran proteins and their complexes were compared; furthermore, the changes in the structural and functional properties of JRBP-CC under different ultrasound conditions were investigated. The results showed that compared with indica rice bran protein (IRBP), the secondary structure of JRBP-CC was very different, the water holding capacity (WHC) was higher, and the emulsification performance was better. Different ultrasound conditions had different effects on the functional properties of JRBP-CC. When the ultrasound power was 200 W, the λmax redshift of the JRBP-CC complex was the most significant, the particle size was the smallest, the absolute value of the zeta potential was the largest, and the hydrophobicity and microstructure of the JRBP-CC complex were the best. Concurrently, the maximum WHC and oil holding capacity (OHC) of JRBP-CC under these conditions were 7.54 g/g and 6.87 g/g, respectively. Moreover, the emulsifying activity index (EAI) and emulsifying stability index (ESI) were 210 m2/g and 47.8 min, respectively, and the scavenging activities of 1,1-diphenyl-2-picrylhydrazyl (DPPH) and ABTS+ were 71.96 % and 80.07 %, respectively.