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peanut allergens Attached with p-Aminobenzamidine Are More Resistant to Digestion than Native allergens

Food and Nutrition Sciences 2016年第14期7卷 1352-1363页

作者： Si-Yin Chung Shawndrika Reed Dunhua Zhang United States Department of Agriculture Agricultural Research Service Southern Regional Research Center New Orleans Louisiana USA United States Department of Agriculture Agricultural Research Service Aquatic Animal Health Research Unit Auburn Alabama USA

Despite being known as resistant proteins, peanut allergens (Ara h 1 and Ara h 2) can be digested and cause allergic reactions. Making the allergens more resistant to digestion may aid in non-absorption and excretion of the allergens. Our objectives were to make Ara h 1 and Ara h 2 more resistant to digestion and test them in a model system using trypsin as the digestive enzyme. The resistant allergens were prepared by covalently attaching p-aminobenzamidine (pABA), a protease inhibitor, to peanut allergens in an extract or on a PVDF membrane using glutaraldehyde, and were then tested for resistance to trypsin digestion. SDS-PAGE and Western blot were performed to determine the allergenic capacity of the modified allergens. A control was prepared using glycine instead. Results showed that Ara h 2, when covalently attached with pABA, was more resistant to trypin digestion than the native allergen. Similarly, Ara h 1, prepared on a PVDF membrane and treated with pABA, displayed a resistance to trypsin digestion. Treatment of the allergens with glycine (a control) instead of pABA showed that the modified allergens were as digestible as native allergens. Blot assays showed that the pABA-treated allergens exhibited a lower allergenic capacity than native allergens. It was concluded that pABA, when attached to peanut allergen Ara h 1 or Ara h 2, inhibited digestion of the allergen by trypsin and reduced their allergenic capacity as well.

关键词： p-Aminobenzamidine peanut allergens Ara h 1 and Ara h 2 Resistance to Digestion

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Effects of different cooking methods on peanut allergenicity

引用

Food Bioscience 2022年第3期47卷 1150-1156页

作者： Tao Wang Yutong Huang Xinlei Tang Hengpeng Wang Bing Li Xiangren Meng Songsong Jiang College of Tourism and Culinary Science Yangzhou UniversityYangzhouJiangsu225127PR China Cuisine Science Key Laboratory of Sichuan Province Sichuan Tourism UniversityChengdu610100PR China Key Laboratory of Chinese Cuisine Intangible Cultural Heritage Technology Inheritance Ministry of Culture and TourismYangzhouJiangsu225127PR China

peanut allergy is a type of serious food allergy *** this study,peanuts were treated with two different cooking *** effect of cooking on digestion stability was evaluated by simulated gastrointestinal *** effects of cooking on the allergenicity were assessed by immunoblotting,passive cutaneous anaphylaxis (PCA) mice model and rat basophilic leukemia (RBL)-2H3 cell *** showed that raw peanuts were more stable to digestion than boiled and fried ***-PAGE showed that the quantities of allergens Ara h 1 (64 kDa),Ara h 2 (20 kDa),and Ara h 3 (38 kDa) in the boiled and fried peanuts were all ***,immunoblotting revealed the IgE binding capacities of boiled and fried peanuts were decreased significantly,especially the fried *** the PCA mice model,the vascular permeability of allergic mice,as well as the release of histamine,were both alleviated in mice gavaged with boiled and fried peanuts compared with raw ***,the release of β-hexosaminidase of RBL-2H3 cells treated with boiled and fried peanuts was significantly decreased compared with the raw *** addition,the analyses of circular dichroism (CD) spectra showed that the α-helical content of peanut proteins was decreased after boiling and frying,indicating the structure stability of peanut allergens *** analyses of ultraviolet (UV) spectra showed that aromatic amino acid residues were exposed,causing the change of the tertiary structure of peanut allergens after boiling and *** conclusion,the allergenicity of peanuts was significantly reduced after boiling and frying,especially frying.

关键词： peanut allergens Cooking methods Allergenicity Protein structure

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