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Compared to conventional high internal phase emulsions (HIPEs), ultrastable HIPEs have recently attracted much attention due to much better stability and protection for bioactive compounds. Here, novel food-grade ultrastable HIPEs were successfully constructed. By simply mixing two individual unstable HIPEs (instability in 3 months in open atmosphere) stabilized by ternary complexes of protein (i.e., lactoferrin), two polyphenols (i.e., (−)-epigallocatechin-3-gallate and curcumin) and two anionic polysaccharides (i.e., κ-carrageenan and low methoxylated pectin), respectively, ultrastable mixed-HIPEs (very stable for 1 year or more in open atmosphere) were achieved unexpectedly. The two individual HIPEs underwent liquid-to-gel and viscous-to-elastic transitions during mixing, exhibiting strong structural synergism. The stabilization was ascribed to the electrostatic repulsive interactions and the formed interpenetrating polymer networks hydrogels in continuous phases; their contribution varied according to the binding sequences of protein, polyphenol, and polysaccharide (for ternary complexes) and the combination modes of individual HIPEs (for mixed-HIPEs). The excellent soft material properties of ternary complexes can provide guarantee for the stsability of emulsion droplets, avoiding their rupture caused by strong squeezing in mixed-HIPEs. This finding greatly expands the type of food grade ultrastable HIPEs. Overall, the novel food-grade ultrastable mixed-HIPEs will offer fascinating opportunities for their future applications in food, medical, cosmetic, and tissue engineering products. • Two high internal phase emulsions (HIPEs) are stabilized by ternary complexes. • Ultrastable HIPEs are achieved by simply mixing two unstable ones. • The stabilization can be mainly ascribed to the electrostatic repulsive interactions. • The interpenetrating polymer networks hydrogels are formed in continuous phases. [ABSTRACT FROM AUTHOR]

Carbon black nanoparticles (CBNPs) and cadmium (Cd) are major components of various air pollutants and cigarette smoke. Autophagy and inflammation both play critical roles in understanding the toxicity of particles and their components, as well as maintaining body homeostasis. However, the effects and mechanisms of CBNPs and Cd (CBNPs-Cd) co-exposure on the human respiratory system remain unclear. In this study, a CBNPs-Cd exposure model was constructed to explore the respiratory toxicity and combined mechanism of these chemicals on the autophagy-lysosome pathway in the context of respiratory inflammation. Co-exposure of CBNPs and Cd significantly increased the number of autophagosomes and lysosomes in human bronchial epithelial cells (16HBE) and mouse lung tissues compared to the control group, as well as the groups exposed to CBNPs and Cd alone. Autophagic markers, LC3II and P62 proteins, were up-regulated in 16HBE cells and mouse lung tissues after CBNPs-Cd co-exposure. However, treatment with Cq inhibitor (an indicator of lysosomal acid environment) resulted in a substantial decreased co-localization fluorescence of LC3 and lysosomes in the CBNPs-Cd combination group compared with the CBNPs-Cd single and control groups. No difference in LAMP1 protein expression was observed among the exposed groups. Adding 3 MA alleviated inflammatory responses, while applying the Baf-A1 inhibitor aggravated inflammation both in vitro and in vivo following CBNPs-Cd co-exposure. Factorial analysis showed no interaction between CBNPs and Cd in their effects on 16HBE cells. We demonstrated that co-exposure to CBNPs-Cd increases the synthesis of autophagosomes and regulates the acidic environment of lysosomes, thereby inhibiting autophagy-lysosome fusion and enhancing the inflammatory response in both 16HBE cells and mouse lung. These findings provide evidence for a comprehensive understanding of the interaction between CBNPs and Cd in mixed pollutants, as well as for the prevention and control of occupational exposure to these two chemicals. • CBNPs and Cd co-exposure increases inflammation in respiratory epithelial cells. • CBNPs and Cd co-exposure targets autophagosome formation and autophagy-lysosomal fusion. • CBNPs and Cd co-exposure disrupts the lysosomal acidic environment. • CBNPs and Cd co-exposure aggravates inflammation by blocking autophagic flux. [ABSTRACT FROM AUTHOR]

• Mulberry anthocyanins shielded β-lactoglobulin against glycation through different mechanisms. • Mulberry anthocyanins dose-dependently mitigated creation of advanced glycation end-products. • Mulberry anthocyanins trapped glyoxal more than methylglyoxal and formed some glyoxal adducts. • Mulberry anthocyanins declined protein-glucose binding and structurally blocked lysyl sites. • Mulberry anthocyanins could be beneficially valorised as functional antiglycation ingredients. Advanced glycation end-products (AGEs), which instigate many disorders, are mostly mediated by dicarbonyl rearrangements. We studied the corresponding mechanisms of the anti-glycation effects of two anthocyanins purified from mulberry fruits, namely cyanidin 3-glucoside (C3G) and cyanidin 3-rutinoside (C3R), on glycated β-lactoglobulins (β-Lg). Both mulberry anthocyanins (MAs) inhibited the AGEs-formation in a dose-dependent manner, but the effect of C3R was significantly stronger than that of C3G (p < 0.05). MAs inhibited AGEs-formation by selectively trapping dicarbonyls, especially glyoxal. The UPLC-ESI-Q-TOF-MS results characterized that C3R formed mono- and di-glyoxal adducts, where C3G only created di-glyoxal adducts. Additionally, C3R could directly interact with some of the glycation sites of β-Lg. Overall, GO-trapping and β-Lg-MAs covalent/noncovalent binding are disclosed as the key mechanisms of the anti-AGEs activity of MAs on β-Lg, which could be valorised as effectual AGEs inhibitors in proteins-rich matrices. [ABSTRACT FROM AUTHOR]