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• Soy protein isolate (SPI) is a major source of functional plant proteins. • The foaming capacity and stability of SPI increased after interaction with rutin. • The nature of the rutin-SPI interaction was characterized using various methods. • The interaction of rutin-SPI was hydrophobic interaction and entropy driven. The aims of present study were to determine the impact of rutin complexation on the ability of soybean protein isolates (SPI) to form and stabilize foams and its mechanism. At pH 7.0, the foaming capacity and foaming stability of the rutin-SPI complexes (28.33% and 14.22%) was appreciably changed when compared with that of SPI alone (19.64% and 32.95%). The improvement in foaming properties was mainly attributed to decrease gas bubble size and increase interfacial thickness as suggested by light microscopy analysis. UV–visible spectroscopy showed that the absorption peak of the SPI was increased and red shifted after complexation with rutin. ITC confirmed that there was an interaction between rutin and SPI. This interaction was hydrophobic interaction and the binding process was entropy driven. This study shows that the foaming properties of plant-based proteins can be improved by forming complexes with flavonoids, which may be useful for foaming agents in foods. [ABSTRACT FROM AUTHOR]

BACKGROUND: Rutin is a natural bioactive flavonoid that is poor in water solubility and chemical stability. Encapsulation can be used to protect bioactive molecules from chemical or physical decomposition during food processing and storage. Thus, the effect of initial particle size on the ability of oil‐in‐water emulsions to retain rutin during storage was investigated. RESULTS: Rutin was encapsulated in oil‐in‐water emulsions with different mean surface‐weighted diameters: d3,2 = 0.56 μm (small), 0.73 μm (medium), and 2.32 μm (large). As expected, the resistance of the emulsions to coalescence and creaming during storage increased as the particle size decreased due to weakening of the colloidal and gravitational forces acting on the droplets. The concentration of rutin in the emulsions decreased during storage (28 days), which was mainly attributed to photodegradation of the flavonoid. The loss of rutin from the emulsions during storage was fitted using a second‐order equation. The rutin degradation rate constant k decreased and the half‐life t1/2 increased with decreasing droplet size, which was attributed to the stronger encapsulation and light scattering by smaller oil droplets reducing the amount of light that can penetrate into the emulsions. CONCLUSION: This study has important implications for the design of more efficacious emulsion‐based delivery systems for incorporating health‐promoting nutraceuticals into foods. © 2022 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

At present, the primary solvents in nanocarrier systems for curcumin encounter challenges related to rapid degradation, and biosafety of organic reagents, surfactants and lipids, which are not suitable for food applications. Therefore, this research proposed an eco-friendly method for the first time, using choline chloride-lactic acid deep eutectic solvent as a solvent for curcumin and a self-assembly medium for short-chain amylose to prepare curcumin-loaded starch nanoparticles. This study investigated the interactions between curcumin and short-chain amylose as well as improved stability. Curcumin was successfully loaded into starch nanoparticles as demonstrated by scanning electron microscopy and confocal laser scanning microscopy analyses. The loading capacity of curcumin-loaded starch nanoparticles on curcumin reached up to 7.99 mg/g, with an encapsulation efficiency of 56.18%. 13C nuclear magnetic resonance spectroscopy peaks at 93–107 ppm and Fourier transform-infrared spectroscopy signals at 3386 cm−1 indicated the formation of a non-inclusion complex through hydrogen bond interactions between curcumin and short-chain amylose. While A-type crystalline pattern and weakening ordered crystallization structure were also probed. Additionally, the formation of non-inclusion complex improved the pH stability and photostability of curcumin through physical barrier of starch nanoparticles and the hydrogen bond interaction between curcumin and starch. Overall, this study established a novel and eco-friendly technique for loading and stabilizing curcumin with nanoscale dimensions, offering potential applications in edible packaging and functional foods. [Display omitted] • Curcumin-loaded starch nanoparticle was firstly prepared via self-assembly in NADES. • Encapsulation by starch nanoparticles enhanced the stability of curcumin. • Curcumin-loaded starch nanoparticle (CSNP) was non-inclusion complex. • CSNP formed by hydrogen bond interaction between curcumin and short-chain amylose. [ABSTRACT FROM AUTHOR]

In present study, the impact of rutin concentration and pretreatment (direct mixing versus pH-driven) of rutin-protein complexes to form and stabilize bilayer emulsions was examined. Bilayer emulsions prepared using the pH-driven method contained smaller oil droplets and had a higher resistance to aggregation and creaming than those prepared using the direct method. The concentration of whey protein isolate at the oil droplet surfaces decreased as the rutin concentration was increased. The oil-water interfacial tension decreased as the rutin concentration in the rutin-whey protein isolate complexes increased, reaching a value of 10.4 mN/m at 0.6 mg/mL rutin. Fluorescence spectroscopy suggested that rutin interacted with the whey protein isolate surfaces mainly through hydrophobic interactions. Moreover, there appeared to be more binding sites and stronger binding interactions when the pH-driven method was used to form the complexes, rather than the direct mixing method. This study suggests that rutin may be used to improve the functional performance of whey protein isolate as emulsifiers in bilayer emulsions. [Display omitted] • Rutin-whey protein isolate (WPI) complexes were prepared. • Rutin-WPI complexes improved the aggregation stability of bilayer emulsions. • Rutin-WPI complexes reduced the interfacial tension at the oil-water interface. • Rutin bound more strongly to whey protein using a pH-driven method. [ABSTRACT FROM AUTHOR]

• Spry-dried oil powders were stabilized by MPI & CHC. • MPI/CHC composites (5:1 or 3:1) gave high encapsulation efficiencies. • MPI/CHC composites protected powdered macadamia oil from oxidation. • Rehydrated emulsions with the highest stability could be produced at MPI/CHC = 5:1. The utilization of oils in the food industry can be facilitated by converting into a powdered form using microencapsulation technologies. In this study, coatings formed from macadamia protein isolate (MPI) and chitosan hydrochloride (CHC) were assessed for their ability to facilitate the microencapsulation of macadamia oil by spray dried, and all encapsulation efficiency was higher than 87.0%. The physicochemical properties of macadamia oil powders were then characterized. In addition, changes in the particle size, aggregation state, and creaming stability of rehydrated emulsions were analyzed during storage. The addition of CHC significantly enhanced the water-solubility and wettability but decreased the flowability of microencapsulated oil. Powdered macadamia oil produced at MPI/CHC = 5:1 had the highest encapsulation efficiency (94.2%), best oxidation stability (<4 meq/kg), and best rehydration properties. Overall, MPI/CHC could be used as a good emulsifier for producing stable rehydrated emulsion, which may therefore be useful in certain food applications. [ABSTRACT FROM AUTHOR]