polyphenol oxidase/hypersensitivitet

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Caffeic acid-assisted cross-linking catalyzed by polyphenol oxidase decreases the allergenicity of ovalbumin in a Balb/c mouse model.

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Ovalbumin (OVA) is the most abundant egg white protein, but is also a major egg allergen. Desensitization of OVA may be a good way to control an egg allergy. In this study, caffeic acid-assisted cross-linked OVA catalyzed by polyphenol oxidase (PPO) was prepared, the effect of cross-linking on the

Emerging food allergens: Identification of polyphenol oxidase as an important allergen in eggplant (Solanum melongena L.).

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Although many allergens have been detected in eggplant (Solanum melongena L.), their identity have not been elucidated. The aim of this study was to investigate whether polyphenol oxidase (PPO), an important eggplant enzyme, acts as an allergen. The proteins of eggplant peel extract were separated

Crosslinking of peanut allergen Ara h 2 by polyphenol oxidase: digestibility and potential allergenicity assessment.

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BACKGROUND Peanut is one of the eight major food allergens. Its allergen, Ara h 2, can be recognized by over 90% of serum IgE samples from peanut-allergic patients. Therefore, reducing the allergenicity of Ara h 2 is especially important. RESULTS In the present study, polyphenol oxidase (PPO), a

Polyphenol-Oxidase-Catalyzed Cross-linking of Ara h 2: Reaction Sites and Effect on Structure and Allergenicity.

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Peanut is among the most common of food allergies, and one of its allergens is Ara h 2. A previous study revealed that this allergen was recognized by serum Ig E in over 90% of a peanut-allergic patient population. Enzymatic cross-linking is a popular processing method used to tailor

Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase.

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Food texture can be improved by enzyme-mediated covalent cross-linking of different food components, such as proteins and carbohydrates. Cross-linking changes the biological and immunological properties of proteins and may change the sensitizing potential of food allergens. In this study we applied

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