In-depth potential mechanism of combined demulsification pretreatments (isopropanol ultrasonic pretreatments and Ca2+ flow additions) during aqueous enzymatic extractions of Camellia oils.

Emulsification is the practical limitation of aqueous enzymatic extractions of Camellia oils. This study aimed to investigate the influence and demulsification mechanisms of isopropanol ultrasonic pretreatments and Ca2+ additions on aqueous enzymatic extractions of Camellia oils. Combining isopropanol ultrasonic pretreatments with Ca2+ flow additions obtained the highest free oil recovery (78.03 %) and lowest emulsion content (1.5 %). Results indicated that the superior demulsification performance originated from the decrease in emulsion stabilities and formations. First, demulsification pretreatments reduced the oil (14.69 %) and solid (13.21 %) fractions in emulsions to decrease the stability of as-formed emulsions. Meanwhile, isopropanol ultrasonic pretreatments extracted tea saponins (0.38 mg/mL) and polysaccharides (0.23 mg/mL), while Ca2+ combined with protein isolates (5.82 mg/mL), tea saponins (7.48 mg/mL) and polysaccharides (0.78 mg/mL) to form precipitates and reduce emulsion formation. This work could promote the practical application of aqueous enzymatic extractions of Camellia oils and enlighten the rise of advanced demulsification pretreatments.

Functional properties of glutelin from Camellia oleifera seed cake: Improvement by alkali-assisted phosphorylation through changes in protein structure.

To explore the effect and its mechanism of alkali-assisted phosphorylation on the functional properties of Camellia Oleifera seeds cake glutelin (CSCG), CSCG was treated with different concentration of sodium trimetaphosphate (STMP, 1.0, 2.0, 3.0, 4.0, and 5%, w/v) in different pH environment (3.0, 5.0, 7.0, 9.0, and 11.0). The results showed that alkali assist improved the phosphorylation degree of CSCG, and the optimum pH value is 9.0. FT-IR and XPS confirmed the successful modification of phosphate groups on CSCG through covalent interaction. Alkali-assisted phosphorylation decreased the particle size and increased electronegativity of CSCG, as well as changed in its surface hydrophobicity, crystallinity, and intrinsic fluorescence. All these changes of protein structure triggered by alkali-assisted phosphorylation led to the improvement of water solubility, water/oil absorption capacity, emulsifying ability, foamability, and in vitro digestibility of CSCG. This work could provide a theoretical basis for industrial production of CSCG with excellent functional properties.

Preparation of novel self-assembled albumin nanoparticles from Camellia seed cake waste for lutein delivery.

The potential utilization value of Camellia seed cake was explored by extracting albumin (CSCA) to develop nanoparticles for lutein delivery. First, thermal property and amphiphilicity of CSCA were evaluated to guide nanoparticle preparation. Next, CSCA nanoparticles modified with chitosan (CS) were prepared through a thermally induced self-assembly method derived by electrostatic attraction and hydrophobic interaction. The optimized nanoparticles were prepared from CSCA:CS at a mass ratio of 2:1 with pH of 4.5, and an incubation temperature and time of 80 ℃ and 10 min, respectively. The nanoparticles had the highest effective loading capacity for lutein at 5.89 ± 0.78%, and the corresponding encapsulation efficiency was 43.82 ± 5.69%. The storage stability of lutein was improved by nanoparticle loading, and the bioaccessibility of lutein in simulated intestinal digestion increased from 26.8 ± 4.4% to 57.3 ± 9.6% after encapsulation into nanoparticles. These findings may facilitate the development of new and sustainable proteins from plant waste for delivery system applications.

Protein isolate from Stauntonia brachyanthera seed: Chemical characterization, functional properties, and emulsifying performance after heat treatment.

The seed of Stauntonia brachyanthera is usually regarded as waste after fructus processing. Here, the potential utilization value of the protein isolate (SSPI) from seeds was evaluated by investigating its physicochemical and functional properties. SSPI was a complex protein containing 7 distinct subunits that had high contents of most essential amino acids. The maximum foaming capacity of SSPI was 406.7 ± 41% at pH 9.0, and the water holding/oil adsorption capacities were 4.66 g/g and 9.06 g/g, respectively. SSPI aggregates with a particle size of 154.1 ± 5.2 nm was prepared after heat treatment, which was performed as a Pickering-like stabilizer for the structuring of water-in-oil-in-water emulsions. The outer droplet size of emulsions decreased as the aggregate concentration increased. Emulsion gels could be observed with the increasing aggregate concentration and oil fraction. Further study found that the stabilities of inner water-in-oil droplets and creaming were progressively increased by increasing the aggregate concentration during storage.