Cold plasma induced amyloid β-lactoglobulin fibrils-fucoidan self-assembled complexes for lycopene delivery: Structural characterization, emulsion stability, and in vitro release behaviour

In this study, a novel delivery system based on self-assembled complexes of amyloid beta-lactoglobulin fibrils (β-LGFs) and fucoidan (FD) was developed to encapsulate and protect lycopene in emulsions. β-LGFs were generated using a cold plasma (CP)-assisted acid-heat induction process under β-LG concentration of 10 mg/mL, CP treatment time of 80 s, and CP power of 60 W. Structural characterization of β-LGFs confirmed the formation of well-defined fibrils and their subsequent interaction with FD at pH 3.0 with a mass ratio of 3:1. The emulsions stabilized by the β-LGF-FD complex exhibited the superior thermal and ultraviolet stability of encapsulated lycopene. The highest retention rate (70.4 %) was obtained in the emulsion with 1.5 wt% β-LGF-FD complex and 50 % oil mass fraction after thermal treatment at 75 °C for 4 h. The increasing the concentration and oil mass fraction could promote the formation of a denser interface layer and more compact gel network structure.