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Sequential high hydrostatic pressure and polyphenol oxidase treatments modulate the structure, digestion behavior,
Weiman Gao1,2, Jingyue Zhang1,2, Lining Ren1,2
1Department of Food Science and Engineering, College of Biological Sciences and Biotechnology, Beijing Key Laboratory of Forest Food Processing and Safety, Beijing Forestry University, Beijing, China.
Background:
Amandin (Pru du 6), a major almond allergen, exhibits immunochemical recognition that is influenced by protein conformation and the accessibility of antibody-recognized regions. This study investigated whether processing sequence governs the effects of high hydrostatic pressure (HHP) and polyphenol oxidase (PPO) on the structural, digestive, and commercial antibody-based immunoreactivity of amandin.
Results:
HHP and PPO conditions were optimized before individual and sequential treatments were compared. Among the tested pressures, 400 MPa produced the lowest commercial antibody-based relative immunoreactivity and was selected for the sequential experiments. HHP pretreatment followed by PPO treatment produced the greatest reduction in antibody-binding immunoreactivity and the most pronounced accumulation of high-molecular-weight material. Spectroscopic and physicochemical analyses showed altered secondary structure, fluorescence behavior, surface hydrophobicity, and sulfhydryl accessibility. Molecular docking supported a potential non-covalent PPO-amandin interaction but was not interpreted as evidence of aggregate formation. HHP-PPO treatment also generated a more interconnected aggregate morphology, increased radical-scavenging activity, and maintained comparatively low antibody-binding immunoreactivity during simulated gastrointestinal digestion despite a lower degree of hydrolysis.
Conclusion:
Processing sequence was a key determinant of amandin structural remodeling and antibody-binding immunoreactivity. The observed structural changes are consistent with HHP pretreatment influencing subsequent PPO-mediated association, although the exact intermolecular linkages and antibody-recognized regions were not determined. Because the enzyme-linked immunosorbent assay used commercial anti-almond-protein antibodies rather than patient immunoglobulin E, further validation with allergic sera and biological models is required before conclusions regarding allergenicity can be made. © 2026 Society of Chemical Industry.
