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Observational analysis reveals enhanced antioxidant activity and reduced allergenicity in Ara h 1 with dynamic ultrahigh pressure and glycation.
The study investigated dynamic ultrahigh pressure (DUHP) combined with galactose/fructose glycation on the structure and properties of Ara h 1. DUHP pretreatment promoted Ara h 1 glycation, with galactose yielding superior results as the carbonyl donor. Conformational changes in glycated Ara h 1 were observed, manifested by the conversion of α-helices to β-sheets, exposure of aromatic amino acid residues, and reduced surface hydrophobicity. Antioxidant and allergenicity analyses revealed that DUHP combined with glycation was more effective than single glycation in enhancing the antioxidant activity and reducing the allergenicity of Ara h 1. Furthermore, galactose was notably superior to fructose in improving these properties. We hypothesized that the potential mechanisms might include: (1) DUHP pretreatment facilitated the generation of heterocyclic compounds, whose increased levels positively correlated with enhanced antioxidant activity; (2) DUHP pretreatment enhanced the covalent binding of Ara h 1 with reducing sugars, inducing changes in both its spatial and primary structures (glycated sites R334, R348, K413, K547 and K559-all located within IgE linear epitopes). These structural modifications disrupted conformational epitopes and masked linear epitopes, consequently reducing its allergenicity. In conclusion, DUHP combined with glycation presents a promising novel strategy for plant protein modification.
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Xu et al. (2025) studied this question.
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