F. Bonomi et al., Advances in the combined application of enzymatic and physical treatments for reducing food allergenicity, HIGH PR RES, 19(1-6), 2000, pp. 565-571
Enzymatic hydrolysis of allergenic food proteins (betalactoglobulin, ovalbu
min) was carried out during treatment at different combinations of time, pr
essure 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 re
sidual intact betalactoglobulin after 10 min at 600 MPa in the presence of
trypsin or chymotrypsin was found to decrease markedly with increasing temp
erature (30-44 degreesC). The temperature sensitivity of the enzymatic hydr
olysis 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 temper
atures (55-65 degreesC), and indicated that complete hydrolysis of betalact
oglobulin cannot be achieved in a short time in the absence of a pressure t
reatment. None of the hydrolysis products of either protein was immunoreact
ive in Western-blot immunoassays.