Journal
FOOD CHEMISTRY
Volume 103, Issue 1, Pages 94-100Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2006.07.029
Keywords
Mal d 1; polyphenol oxidase; peroxidase; antioxidants; competitive ELISA
Ask authors/readers for more resources
Mal d 1, the major apple allergen, is heat labile and easily oxidized. Oxidative reactions catalyzed by polyphenol oxidase (PPO) and/or peroxidase (POD), present in apple, may be involved in decreasing its allergenicity. PPO and POD convert phenolic compounds into o-quinones. In this study the effect of PPO and POD, the polyphenol catechin and the antioxidant DIECA on IgE-binding by Mal d I was analyzed. Golden Delicious peel was selected for its high PPO and POD contents. IgE-binding was analyzed by competitive ELISA. IgE-binding by Mal d I decreased by adding oxidative enzymes, this decrease was most pronounced when PPO was used. Catechin induced a reduction in IgE binding when POD was used. The combination of catechin and PPO causes the strongest decrease of the allergenicity of Mal d 1. DIECA protected the IgE-binding by the allergen, protection being less strong in the presence of exogenous PPO and POD. The decrease of immunoreactivity is likely to be due to o-quinones, as active species or other intermediates modifying the tertiary structure of the allergens and cross-linking of the proteins, thus reducing their allergenicity. (c) 2006 Elsevier Ltd. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available