As a globally cultivated and economic crop, beets are particularly important in the cane sugar and feed industries. Beet pigments are among the most important natural pigments, while various chemical components in beets display beneficial biological functions. Phenolic substances and betalains, as the main bioactive compounds, determine the functional characteristics of beets. This review categorizes the basic types of beets by the chemical composition of bioactive substances in their leaves, stems, and roots and emphatically summarizes the research progress made on the functions of two major substances in different types of beets: phenolic compounds and betalain pigments. This study provides useful insights for the comprehensive and effective application of beets in the health food and pharmaceutical industries.

Zein was made flexible through acid-driven deamidation. This increased flexibility was confirmed by the higher release of water-soluble peptides during trypsin hydrolysis. Self-assembled flexible zein nanoparticles (FZNPs) were prepared using the anti-solvent precipitation method. To test the sensitivity of FZNPs to complex environment, ionic solutions (CaCl₂ and NaCl) at various concentrations were prepared. The morphology and particle size of FZNPs differed significantly from those of control zein nanoparticles (NZNPs). As the ionic concentration increased from 0 to 15 mmol/L, FZNPs showed higher electrical conductivity and adsorption capacity than NZNPs. This suggests that FZNPs are highly sensitive to complex environment. X-Ray Photoelectron Spectrum (XPS) results revealed that both FZNPs and NZNPs bound more Na⁺ than Ca²⁺. The enhanced sensitivity of FZNPs to complex environments may be due to their greater tendency for structural changes. These conformational changes are likely caused by the altered amino acids in flexible zein, which result from deamidation. This study offers a practical approach to designing novel nanoparticles as functional materials for delivering bioactive compounds.

Nuclei refers to the intermediate product formed at the initial stage of protein fibril aggregation, which has a high activation energy, stable structure, and is resistant to hydrolysis. Nuclei was obtained from fibrillar whey protein isolate. Zein-nuclei core-shell nanoparticles were utilized to encapsulate curcumin. As the ratio of zein to curcumin decreased from 40:1 to 4:1, the particle size increased from 144.77 to 157.00 nm, accompanied by morphological transition from stranded to spherical structure. The optimal zein-to-curcumin ratio was 10:1, at which the complex exhibited the highest encapsulation efficiency (92.65%) and loading capacity (8.35%). Complex formation was driven by hydrogen bonding, electrostatic interactions, and hydrophobic effects. Moreover, the addition of curcumin induced structural modifications in the zein-nuclei binary complexes, which in turn influenced their thermal stability. The thermal stability of curcumin were significantly enhanced upon encapsulation within the zein-nuclei core-shell nanoparticles. Moreover, the release of curcumin was markedly delayed in simulated gastrointestinal fluids when encapsulated in these complexes. These findings demonstrate that zein-nuclei core-shell nanoparticles represent a promising encapsulation system for curcumin in the food industry.

To investigate the respective contributions of cations (Na⁺, K⁺, Zn²⁺, Fe³⁺) and anions (Cl⁻ and SO₄²⁻) to the formation of whey protein isolate (WPI)-based nanofibrils, eight salts with a 4 × 2 factorial design were added to WPI solutions. The morphology and aggregation process of the fibril aggregates were examined under fixed low salt concentration (10 mmol/L) to isolate ion-specific effects. The salts altered the pH, conductivity, and fibril yield. Notably, the Na⁺, K⁺, and Zn²⁺ salts increased fibril production, whereas Fe³⁺ salts reduced it. Mechanistically, Fe³⁺ strongly suppressed fibrillation via strong electrostatic interaction and accelerated protein hydrolysis, while SO₄²⁻ partially alleviated this inhibition. All the ions altered the kinetic parameters. Compared with Cl⁻ salts, SO₄²⁻ salts induced shorter, clustered fibrils and stronger kinetic suppression, preserving elongated fibrils. X-ray photoelectron spectroscopy (XPS) confirmed anion incorporation, and X-ray diffraction (XRD) revealed secondary structural changes. These results demonstrate that while cations contribute to fibril formation, anions play a deterministic role in regulating assembly kinetics and morphological outcomes, independent of cation valence. In this study, we establish a mechanistic basis for tailoring WPI fibril aggregation states through anion-specific salt selection.