Characterization of the molecular properties and allergenicity (IgE-binding capacity) of β-lactoglobulin by heat treatment using asymmetric-flow field-flow fractionation and ultra-performance liquid chromatography quadrupole time of flight mass chromatography

Reducing Antigenicity and Improving Antioxidant Capacity of β-Lactoglobulin through Covalent Interaction with Six Flavonoids

“…β-LG is a highly valuable protein for its rich nutrition and emulsifying and foaming properties, so it is often used as a functional additive in a variety of industries [5]. However, β-LG is a prominent milk allergen, with approximately 82% of individuals with milk protein allergies experiencing an allergic reaction to β-LG [6]. Furthermore, β-LG exhibits limited antioxidant capacity, which compromises its ability to counteract oxidative species, thereby leading to structural, functional, stability, and nutritional alterations [7].…”

Heat-induced structural modifications of plant proteins : Implications for peptide pattern and bioactivity after infant digestion

“…However, denaturation and aggregation may occur during these steps, as well as glycation in the presence of reducing sugars, resulting in potential alteration of epitopic properties, hence differences in immunogenicity of these proteins. For instance, heating can increase allergenicity by inducing protein unfolding and aggregation exposing new epitopes (Li, Yang, Zou, Shu, Han, & Yang, 2022;. On the other hand, heating can also decrease allergenicity through glycation, which involves the formation of soluble aggregates and/or covalent modification on lysine and arginine residues within epitopes, resulting in a reduced capacity for IgE binding (Bai et al, 2021;.…”