Exploring the potential of enzymatic hydrolysis assisted glycosylation to modify β-lactoglobulin fibrils: Insights into aggregation behavior, functional properties and antibody binding capacity.

This study investigated the effects of enzymatic hydrolysis and glycosylation on the self-assembly and functional properties of β-lactoglobulin (β-LG) amyloid fibrils. Thioflavin T fluorescence spectroscopy confirmed the successful formation of amyloid fibrils from modified β-LG samples. Transmission electron microscopy observations revealed that β-LG, hydrolyzed β-LG, and glycosylated-hydrolyzed β-LG formed relatively long fibrils (Fβ-LG), a coexistence of long and short fibrils (FHβ-LG), and a fibril system that was shorter than Fβ-LG (FGHβ-LG), respectively. FGHβ-LG exhibited significantly enhanced emulsifying properties, antioxidant capacity, and foaming capacity compared to β-LG. Moreover, these aggregates remarkably reduced the IgE and IgG binding to β-LG. Amino groups exposed during enzymatic hydrolysis promoted glycosylation efficiency, while the conjugated glycosyl chains regulated the surface hydrophilicity of the fibrils. In summary, this sequential modification expands the potential applications of β-LG fibrils as functional food ingredients and emulsifiers in food systems.