Characterization of high-pressure-treated egg albumen

Addition of NaCl or sucrose to egg albumen prior to high-pressure treatment (up to 10 min at 800 MPa) prevented insolubilization or gel formation afte r pressure treatment. As a consequence of protein unfolding, the treated al bumen had increased viscosity but retained its foaming sind heat-gelling pr operties. Susceptibility of egg albumen proteins to hydrolysis by trypsin i ncreased dramatically after pressure treatment. The S-form of ovalbumin, th e presence of which is an index of egg aging, was not found in any of the p ressure-treated samples, which also did not display evidence for covalent p rotein aggregation. However, recognition of ovalbumin by an anti-ovalbumin antiserum was reduced to 40% of that of untreated sample.