The effects of high pressure on the solubility and on some structural features of ovalbumin were
investigated on protein solutions at neutral pH, containing different protein concentrations and
treated at 400−800 MPa for different times. Ovalbumin solutions were prepared in the presence
and in the absence of common food ingredients, such as sucrose and NaCl, that could act as
“protectants” against treatment-induced modification. Protein insolubilization occurred in the
absence of protectants as a function of the protein concentration and the treatment intensity; it
appeared to be a consequence of structural modifications involving in particular the tertiary structure
of the protein, and it was completely prevented by blocking the free −SH groups in the protein.
Several of the structural features of the protein were modified also when it was treated in the
presence of protectants. Modifications depended on the treatment pressure and time and on the
protectant used. All of the treated proteins showed an increased susceptibility to proteolysis by
trypsin and a decrease in the recognizability by specific antibodies. These effects were particularly
evident when treatments were performed in the presence of sucrose, which was less effective than
NaCl in preventing structural modifications upon treatment.
Keywords: Ovalbumin; high pressure; protein structure; digestibility; food allergenes
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