No abstract

Unacceptable bitter taste limits the application of luteolin in healthier food systems. In this study, the bitterness-masking assessment was performed on the whey protein isolate-coated liposomes loaded with luteolin (WPI-coated...

Summary Naringin has various biological activities with an unacceptable bitter taste. In this work, pea protein–naringin complexes (PP–NG complexes) were constructed to stabilise the Pickering emulsion and reduce the bitterness of naringin. Sensory evaluation results showed that the bitterness and after‐bitterness of the PP–NG complexes were reduced by 77.78% and 75.99% compared with 1 mm naringin respectively. For the PP–NG complexes, the fluorescence spectra results showed that the endogenous fluorescence intensity of pea protein decreased with the naringin concentration increased (0–2 mm), and each pea protein molecule bound to one naringin molecule. Results obtained via thermodynamic analysis molecular docking demonstrated that naringin had an excellent binding affinity (−7.4 kcal mol−1) with pea protein and could form five hydrophobic bonds and four hydrogen bonds with pea protein. These findings would provide a new idea for the masking of bitterness and the evolution of Pickering emulsions stabilised by the protein–polyphenol nanoparticles.