Combined effect of high pressure and temperature on selected properties of egg white proteins

TLDR: In this article, the effect of pressure at different temperature (10, 25, and 60 °C) and pH (7.6 and 8.8) levels on selected properties of egg white solutions (turbidity, solubility, residual denaturation enthalpy, surface hydrophobicity, sulfhydryl content, susceptibility to enzymatic hydrolysis and trypsin inhibition activity).

Abstract: A study was conducted on the effect of pressure at different temperature (10, 25, and 60 °C) and pH (7.6 and 8.8) levels on selected properties of egg white solutions (turbidity, solubility, residual denaturation enthalpy, surface hydrophobicity, sulfhydryl content, susceptibility to enzymatic hydrolysis and trypsin inhibition activity). The pressure-induced changes in these properties were dependent on the pressure and temperature applied and the pH. The most pronounced changes were observed in the pressure range of 400–700 MPa. Pressure induced an increase in turbidity, surface hydrophobicity, exposed SH content and susceptibility to enzymatic hydrolysis, while it resulted in a decrease in protein solubility, total SH content, denaturation enthalpy and trypsin inhibitory activity. Industrial relevance Egg white is a multifunctional food ingredient with unique properties. Since pressure can induce changes in protein functionality it is of industrial relevance to explore the impact of pressure at different temperatures on egg white properties. Pressure induced changes were pronounced and also dependent on pH and temperature thus offering the potential for a wide range of p, T and pH combinations for monitoring of unique egg white protein functionality.