Abstract
This work describes the effect of isostatic pressure 500 MPa on tryptic and chymotryptic hydrolysis of α- and β-casein, bovine serum albumin (BSA), β-lactoglobulin (β-Lg) and α -lactalbumin (α-La). Digestion was also conducted at atmospheric pressure. The extent of hydrolysis and peptide profiles were analysed by gel-permeation and reverse-phase high-performance liquid chromatographies. The residual immunochemical reactivities of the protein hydrolysates were assessed by the Streptavidin ImmunoCAP system (Phadia) for determination of specific immunoglobulin type E (IgE) antibodies. We have found very significant changes of the peptide profiles and a progressive reduction in residual-intact proteins after applying high pressure during tryptic proteolysis of β-Lg and BSA and chymotryptic proteolysis of β-Lg, α-La and BSA. A statistically significant decrease of the residual immunochemical reactivities of β-Lg tryptic and α-La chymotryptic hydrolysates prepared under high pressure, in comparison with the control samples hydrolysed at atmospheric pressure, was also observed.
Acknowledgements
This work was supported by research grant 2B06174 of the National Research Programme II.