In this paper, the food-grade gelatin nanoparticles (GNPs) were prepared by a two-step desolvation method and using genipin as a cross-linker. The GNPs with narrow size distribution and good dispersion could be obtained only at pH 12. The effect of the genipin dosage (8–12 wt%) on the GNPs was systematically investigated. The results showed that the cross-linking degree of the GNPs increased with the increasing dosage of genipin, thus leading to a more obvious cross-linking morphology observed from scanning electron microscope (SEM). The obtained GNPs showed a good dispersibility with a size range of 386–438 nm. However, the GNPs cross-linked by 8 wt% genipin dosage revealed a relatively higher size because of the aggregation induced by hydrogen bond. The 10 wt% group had good thermal stability and storage stability. The optical microscopy results showed that the Pickering emulsions (30–50 vol% internal phase) stabilized by the GNPs had good uniformity and stability, even after 30 days of storage time, suggesting that the stable GNPs had great potential in food-grade Pickering emulsions.

Polysaccharide hydrocolloids have garnered increasing attention from consumers, experts, and food processing industries due to their advantages of abundant resources, favorable thickening properties, emulsification stability, biocompatibility, biodegradability, and high acceptance as food additives. This review focuses on the application of polysaccharide hydrocolloids and their beneficial roles in meat products by focusing on several commonly used polysaccharides (i.e., cellulose, chitosan, starch, sodium alginate, pectin, and carrageenan). Firstly, the recent advancements of polysaccharide hydrocolloids used in meat products are briefly introduced, along with their structure and potential application prospects. Then, the beneficial roles of polysaccharide hydrocolloids in meat products are comprehensively summarized and highlighted, including retarding lipid and protein oxidation, enhancing nutritional properties, improving texture and color quality, providing antibacterial activity, monitoring freshness, acting as a cryoprotectant, improving printability, and ensuring security. Finally, the challenges and opportunities of polysaccharide hydrocolloids in meat products are also introduced.

Aflatoxin B₁ (AFB₁) is a highly toxic mycotoxin found worldwide in cereals, food, and animal feeds. AFB₁ binds to human serum albumin (HSA) with high affinity. In previous experiments, it has been revealed that reducing the binding rate of AFB₁ with HSA could speed up the elimination rate of AFB₁. Therefore, we examined the ability of quercetin to compete with AFB₁ for binding HSA by fluorescence spectroscopy, synchronous spectroscopy, ultrafiltration studies, etc. It was shown that AFB₁ and quercetin bind to HSA in the same Sudlow site I (subdomain IIA), and the binding constant (K_a) of the quercetin-HSA complex is significantly stronger than the complex of AFB₁-HSA. Our data in this experiment showed that quercetin is able to remove the AFB₁ from HSA and reduce its bound fraction. This exploratory work may be of significance for studies in the future regarding decreasing its bound fraction and then increasing its elimination rate for detoxification. This exploratory study may initiate future epidemiological research designs to obtain further in vivo evidence of the long-term (potential protective) effects of competing substances on human patients.

Dietary protein supplementation has emerged as a promising strategy in combating sarcopenia. Furthermore, searching for alternatives of animal proteins has been a hot topic. The present study aimed to investigate the effects of zein peptides on C₂C₁₂ myoblasts and explore their potential molecular mechanisms. The proliferative, cell cycle, and anti-apoptotic activities of zein peptides were evaluated. Peptidomics analysis and transcriptome sequencing were employed to explore the structure-activity relationship and underlying molecular mechanisms. The results indicated that zein peptides (0.05–0.2 mg/mL) exerted a significant proliferation-promoting impact on C₂C₁₂ cells, via increasing cell viability by 33.37 to 42.39%. Furthermore, zein peptides significantly increased S phase proportion and decreased the apoptosis rate from 34.08% (model group) to 28.96% in C₂C₁₂ cells. In addition, zein peptides exhibited a pronounced anti-apoptotic effect on C₂C₁₂ cells. Zein peptides are abundant in branch-chain amino acids, especially leucine. Transcriptomics analysis revealed that zein peptides can promote proliferation, accelerate cell cycle, and improve protein synthesis of muscle cells through mTORC1 and mTORC2 signaling pathways.

α-zearalenol (α-ZOL) is a mycotoxin with a strong estrogen effect that affects the synthesis and secretion of sex hormones and is transported to target organs through human serum albumin (HSA). Additionally, it has been reported that curcumin can also bind to HSA with high affinity at the same binding site as α-ZOL. Additionally, several studies reported that reducing the bound fraction of α-ZOL contributes to speeding up the elimination rate of α-ZOL to reduce its hazard to organs. Therefore, to explore the influence of a nutrition intervention with curcumin on α-ZOL effects, the competitive displacement of α-ZOL from HSA by curcumin was investigated using spectroscopic techniques, ultrafiltration techniques and HPLC methods. Results show that curcumin and α-ZOL share the same binding site (subdomain IIA) on HSA, and curcumin binds to HSA with a binding constant of 1.12 × 10⁵ M⁻¹, which is higher than that of α-ZOL (3.98 × 10⁴ M⁻¹). Ultrafiltration studies demonstrated that curcumin could displace α-ZOL from HSA to reduce α-ZOL’s binding fraction. Synchronous fluorescence spectroscopy revealed that curcumin could reduce the hydrophobicity of the microenvironment of an HSA–α-ZOL complex. This study is of great significance for applying curcumin and other highly active foodborne components to interfere with the toxicokinetics of α-ZOL and reduce its risk of its exposure.

In this paper, an electrochemical biosensor was established for the high-sensitivity detection of Tenuazonic acid (TeA) in fruits based on the enrichment of flower-shaped nano-ZnO and the specific recognition of immune response. Herein flower-shaped nano-ZnO (ZnO NFs) with a hexagonal wurtzite structure and diameter of 700–800 nm were demonstrated to have the optimal specific surface area and outstanding conductivity, compared with different morphology, sizes, and crystal structures of nano-ZnO. Second, the ZnO NFs were used as carriers for efficiently immobilizing monoclonal antibodies to obtain antibody bioconjugates, which were anchored on the 2-mercaptobenzoic acid-modified gold electrode by amide reaction. In the presence of TeA, the monoclonal antibody could specifically recognize and bind to it, resulting in a decrease in electron transfer ability on the gold electrode surface. Finally, the electrochemical biosensor showed a range from 5 × 10⁻⁵ μg/mL to 5 × 10⁻¹ μg/mL with a detection limit of 1.14 × 10⁻⁵ μg/mL. Furthermore, it exhibited high selectivity for TeA among other analogs, such as Altenuene (ALT) and Alternariol (AOH). Notably, the proposed strategy could be employed to monitor TeA in tomato and citrus, showing potential application prospects in practical application and commercial value.