Due to their combination of featured properties, protein and polysaccharide-based carriers show promising potential in food bioactive ingredient encapsulation, protection, and delivery. The formation of protein–polysaccharide complexes and conjugates involves non-covalent interactions and covalent interaction, respectively. The common types of protein–polysaccharide complex/conjugate-based bioactive ingredient delivery systems include emulsion (conventional emulsion, nanoemulsion, multiple emulsion, multilayered emulsion, and Pickering emulsion), microcapsule, hydrogel, and nanoparticle-based delivery systems. This review highlights the applications of protein–polysaccharide-based delivery vehicles in common bioactive ingredients including polyphenols, food proteins, bioactive peptides, carotenoids, vitamins, and minerals. The loaded food bioactive ingredients exhibited enhanced physicochemical stability, bioaccessibility, and sustained release in simulated gastrointestinal digestion. However, limited research has been conducted in determining the in vivo oral bioavailability of encapsulated bioactive compounds. An in vitro simulated gastrointestinal digestion model incorporating gut microbiota and a mucus layer is suggested for future studies.

The effect of different degree of hydrolysis (DH) by Alcalase on the structural and interfacial properties of sunflower protein isolates was investigated. Sunflower protein isolates were extracted from defatted sunflower flour and hydrolyzed by Alcalase by applying different DH (low [10%], medium [20%] and high [30%]). Size exclusion chromatography results showed that the sunflower protein hydrolysates with different low molecular mass distribution were detected. Circular dichroism analysis showed the hydrolysates possessed a decreased α-helix but higher β-turn and random coil structures. The analysis of intrinsic fluorescence spectra indicated a moveable tertiary conformation of the hydrolysates. In comparison with sunflower protein isolate, its hydrolysates showed higher foaming activity and emulsion stability, but the foams were unstable and the emulsifying activity index was decreased. The hydrolysis significantly modified the structural and interfacial properties of the sunflower protein isolate. The structural and interfacial properties of sunflower protein isolates were remarkably modified by the Alcalase hydrolysis with the DH range of 10–30%. The hydrolysates exhibited relatively higher foaming capacity and emulsion stability index. Limited hydrolysis and excessive hydrolysis of sunflower protein isolates can enhance foaming capacity and emulsion stability of the products. Thus it was demonstrated that by controlling DH of sunflower protein isolates, hydrolysate with a desirable functional properties can be obtained.

Background: Unreasonable use of antibiotics in animals is a major concern and will remain so, thus affecting people's health. However, the application of plant extracts can better solve this problem.Objectives: The purpose of this study was to study the effect of Moringa leaf flavonoids on the production performance, immunity, and rumen fermentation of dairy cows.Methods: Nine Holstein multiparous cows (average weight: 550 kg; days of lactation: 150 ± 6 days) were used in the experiment, using a 3 × 3 Latin square design. Cows were divided into three groups, each of which was supplemented with 0, 50, or 100 mg/body weight (BW) Moringa oleifera leaf flavonoids. Each experimental period consisted of three periods of 21 days, and the prefeeding period lasted 15 days.Results: Our results indicated that supplementation with Moringa leaf flavonoids increased the protein content and decreased the number of somatic cells in milk; had little effect on the biochemical indices of blood, the rumen fermentation, and serum biochemical indicators; and improved the activity of antioxidant enzymes, the antioxidant capacity, and immunity.Conclusions: Addition of 50 mg/BW Moringa leaf flavonoids to cow enhanced the antioxidant and immunity capacity in dairy cows but did not affect physiological levels of common biochemical parameters in blood or fermentation parameters in rumen.

The effects of hot air temperature and slice thickness on the drying kinetics and quality of Hami melon slices (HMS) were studied. HMS (3 mm and 5 mm) were carried out in a forced convection drying oven at temperatures ranging from 60 ~ 90 °C. The increase in hot air temperature and the decrease in slice thickness led to shorter drying times and higher drying rates. The drying rate curves indicated that the drying process of HMS did not exhibit a constant drying rate period. In the drying kinetics modeling process, the Explinear model was suited for describing the drying curves with higher accuracy. According to Fick’s second law, the moisture effective diffusion coefficient of 3 mm and 5 mm HMS ranged from 4.72 ~ 15.96 × 10^-11m²/s at temperatures of 60, 70, 80, and 90 °C. When the thickness of HMS were 3 mm and 5 mm, the activation energies were 30.13 and 43.75 kJ/mol, respectively. When dried at low temperatures, the color of HMS was closer to fresh Hami melon. With the increase of hot air temperature, the hardness of HMS decreases and the rehydration increases. When the thickness of the HMS decreases, the hardness of the slices decreases and the rehydration increases.

New glycopeptides were generated by proteolysis from corn gluten meal (CGM) followed by transglutaminase (TGase)-induced glycosylation with glucosamine (GlcN). The glycopeptides exhibited desirable antioxidant and intracellular ROS-scavenging properties. The amount of conjugated GlcN quantified by high-performance liquid chromatography (HPLC) was 23.0 g/kg protein. The formed glycopeptides contained both glycosylated and glycation types, as demonstrated by the electrospray ionization time-of-flight mass spectrometry (ESI-TOF MS/MS). The glycopeptides exhibited scavenging capabilities against free radical diphenylpicrylhydrazyl (DPPH) and hydroxyl radicals by reducing their power. The potential protection of glycopeptides against ethanol-induced injury in LO2 cells was assessed In Vitro based on methyl thiazole tetrazolium (MTT) testing and intracellular reactive oxygen species (ROS) scavenging capacity, respectively. Glycopeptide cytoprotection was expressed in a dose-dependent manner, with the glycopeptides exhibiting good solubility ranging from 74.8% to 83.2% throughout a pH range of 2–10. Correspondingly, the glycopeptides showed good emulsifying activity (36.0 m²/g protein), emulsion stability (74.9%), and low surface hydrophobicity (16.3). These results indicate that glycosylation of CGM significantly improved its biological and functional properties. Glycopeptides from CGM could be used as potential antioxidants as well as comprising a functional food ingredient.