Abstract

Egg is the second most common food allergen among infants and young children. This work investigated the influence of plastein reaction on immunoglobulin E (IgE)-binding activities of egg white protein hydrolysates after simulated gastrointestinal (GIT) digestion. Compared to hydrolysate precursors, the IgE-binding activity of Pepsin-Plastein significantly decreased from 35 ± 7% to 8 ± 2% (P < 0.05), and Papain-Plastein from 70 ± 5% to 59 ± 4%. Further GIT hydrolysis of Pepsin-Plastein maintained the reduced IgE-binding activity (7 ± 3%) whereas Papain-Plastein digestion restored the IgE-binding reactivity to 66 ± 7%. This discrepancy is related to the different mechanisms of plastein formation. Covalent modifications (decreased free amino nitrogen and sulfhydryl contents) provided biostability for Pepsin-Plastein, whereas hydrophobic interactions (increased surface hydrophobicity) mainly contributed to Papain-Plastein formation. The latter can be destroyed during GIT digestion leading to re-exposure of hidden IgE-binding epitopes. Taken together, plastein reaction is a promising strategy for inducing structural modifications that reduce the immune reactivity of allergenic proteins.

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