Aggregation and conformational changes of bovine β-lactoglobulin subjected to dynamic high-pressure microfluidization in relation to antigenicity

Abstract

Our previous research indicated that dynamic high-pressure microfluidization (DHPM) had a significant effect on the antigenicity of β-lactoglobulin (β-LG). In this study, aggregation and conformational changes subjected to DHPM (0.1-160 MPa) were investigated in relation to antigenicity. When DHPM pressure increased from 0.1 to 80 MPa, disaggregation of β-LG samples and partial unfolding of the molecule were accompanied by an increase in β-LG antigenicity, which was reflected in the decrease of particle size, increase of free sulfhydryl (SH) contents and β-strands contents, and slight exposure of aromatic amino acid residues. At pressures above 80 MPa, the reaggregation of β-LG may contribute to the decrease in antigenicity, which was reflected by an increase in particle size, the formation of aggregates, a decrease of in SH and β-strands contents, and slight changes in aromatic amino acid residues. Aggregation and conformational changes of β-LG under DHPM was related to its antigenicity.