The mechanism by which thermal/pressure processing influences the allergenicity of shrimp (Penaeus vannamei) was explored by
anaphylaxis in mice, the
protein structure, gastrointestinal digestion, and linear
epitopes. Roasting induced the unfolding of the structure, which may reduce the allergenicity, but it made more linear
epitopes to be exposed, causing mice to exhibit similar systemic
anaphylaxis as mice fed with the raw shrimp
protein (p > 0.05). However, the roasted + reverse-pressure-sterilized shrimp can significantly reduce specific
antibodies, mast cell degranulation, vascular permeability, and histopathological morphology in mice compared with the raw and roasted shrimp (p < 0.05) because reverse-pressure sterilization causes
protein to aggregate, hiding the heat/digested stable
epitopes of
arginine kinase (Glu59-Ser63, Asn112-Lys118, Leu131-Phe136, and Ser158-Glu162) and sarcoplasmic
calcium-binding protein (Asn57-Phe67, Ser159-Cys165, and Glu126-Ala130) inside a 3D structure, while gastrointestinal digestion can destroy immunodominant, minor
epitopes and the
epitopes exposed by roasting. Meanwhile, the low binding frequency of
IgE to
troponin C was also responsible for maintaining the hypoallergenicity of shrimp.