The intestinal epithelial barrier plays a key protective role in the gut lumen. Bovine lactoferrin (bLF) has been reported to improve the intestinal epithelial barrier function, but its impact on tight junction (TJ) proteins has been rarely described. Human intestinal epithelial crypt cells (HIECs) were more similar to those in the human small intestine, compared with the well-established Caco-2 cells. Accordingly, both HIECs and Caco-2 cells were investigated in this study to determine the effects of bioactive protein bLF on their growth promotion and intestinal barrier function. The results showed that bLF promoted cell growth and arrested cell-cycle progression at the G2/M-phase. Moreover, bLF decreased paracellular permeability and increased alkaline phosphatase activity and transepithelial electrical resistance, strengthening barrier function. Immunofluorescence, western blot and quantitative real-time polymerase chain reaction revealed that bLF significantly increased the expression of three tight junction proteins—claudin-1, occludin, and ZO-1—at both the mRNA and protein levels, and consequently strengthened the barrier function of the two cell models. bLF in general showed higher activity in Caco-2 cells, however, HIECs also exhibited desired responses to barrier function. Therefore, bLF may be incorporated into functional foods for treatment of inflammatory bowel diseases which are caused by loss of barrier integrity.

Chlorogenic acid (CGA), a polyphenolic compound found in various plant species, has shown considerable potential in the treatment and management of several diseases due to its potent bioactive properties.

Amyloid fibrillization represents an effective strategy for extending and enhancing protein function, particularly for the delivery of hydrophobic active substances. In this study, oat globulin (OG) and its fibrils were complexed with quercetin (Que) to construct the delivery system, and ultrasonic pretreatment was applied during fibril preparation to explore the promoter of complex formation. The results demonstrated that complexation with Que induced a dose-dependent static quenching of the intrinsic fluorescence of the protein/fibrils, with hydrophobic interactions and tryptophan residues being the primary interaction forces and the main fluorescence quenching groups, respectively. In comparison, OG fibrils prepared with ultrasound pretreatment (UOGF) exhibited the strongest encapsulation and loading capacity for Que, ranging from 97.16% at a mass ratio of 200:1 to 42.48% at a ratio of 25:1. Subsequently, complexes were prepared with a ratio of 50:1. Structural analysis revealed that Que primarily interacts with the protein/fibril carriers through hydrogen bonds and hydrophobic interactions, inducing structural changes and ultimately being encapsulated in an amorphous form within the composite material. Additionally, Que promoted the mutual aggregation and cross-linking of protein/fibril units, leading to increased hydrodynamic diameter and zeta-potential. Moreover, UOGF-Que showed the greatest improvement in the thermal stability and the photostability of Que, and enhancing the bioaccessibility. These findings provide valuable insights into using ultrasound as an auxiliary measure for fibril self-assembly to enhance the application potential of fibrils, especially the delivery of hydrophobic functional substances.