Advances in the combined application of enzymatic and physical treatments for reducing food allergenicity

Abstract

Enzymatic hydrolysis of allergenic food proteins (betalactoglobulin, ovalbumin) was carried out during treatment at different combinations of time, pressure and temperature, with the aim of hydrolyzing the protein conformers transiently formed in the course of physical treatment in conditions where no irreversible modification of the target protein occurs. The amount of residual intact betalactoglobulin after 10min at 600 MPa in the presence of trypsin or chymotrypsin was found to decrease markedly with increasing temperature (30–44°C). The temperature sensitivity of the enzymatic hydrolysis of ovalbumin during similar treatments was much less pronounced than that of betalactoglobulin. The effects of temperature on the accessibility of betalactoglobulin conformers to proteases were studied at higher temperatures (55-65°C), and indicated that complete hydrolysis of betalactoglobulin cannot be achieved in a short time in the absence of a pressure treatment. None of the hydrolysis products of either protein was immunoreactive in Western-blot immunoassays.