Abstract
The effect of high pressure homogenisation (HPH) on decontamination, protein structure (turbidity, particle size, free sulfhydryl groups, protein electrophoretic mobility) and selected functional properties (immunoreactivity, viscosity, foaming and gelling properties) of egg white were evaluated. HPH at 150MPa for multiple passes allowed the progressive inactivation of Salmonella enterica SDMZ 9898. In addition, HPH modified egg white proteins by inducing unfolding and aggregation phenomena. The latter would occur by means of hydrophobic interactions among partially unfolded proteins. Protein structure modifications induced by HPH decreased egg white immunoreactivity probably due to protein epitopes hiding upon aggregation. HPH was not sufficient to modify egg white foaming properties. Depending on the intensity of the process, HPH allowed the modification of apparent viscosity of egg white and firmness of egg white gel.
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