Studying the effects of high pressure–temperature treatment on the structure and immunoreactivity of β-lactoglobulin using experimental and computational methods

Abstract

The effects of high hydrostatic pressure (HHP) on the conformation and immunoreactivity of bovine β-lactoglobulin (BLG) were studied. BLG was treated under 100–600 MPa at the temperature of 20–60 °C. The immunoglobulin E (IgE) binding ability of BLG decreased when the pressure increased from 0.1 to 200 MPa. However, the IgE binding increased with the increase in pressure from 200 to 400 MPa, followed by a gradual decrease until a pressure of 600 MPa. The IgE binding ability continuously decreased with an increase in pressure at 60 °C. The conformation of HHP-treated BLG was evaluated using fluorescence spectroscopy, circular dichroism spectroscopy and molecular dynamics (MD) simulation. Increasing the temperature and pressure promoted the unfolding of BLG, causing the disappearance of some α-helixes and some β-sheets. Based on ELISA analysis, it was revealed that HHP-termperature treatment altered the immunoreactivity of BLG by altering the structures and conformational states of BLG.