title: Thermal processing effects on peanut allergen Ara h 2 allergenicity in mice and its antigenic epitope structure.
abstract: Ara h 2 was purified from peanuts that were thermally treated by various processes, including boiling, glycation, frying and roasting. The allergenicity of Ara h 2 in Balb/c mice and the influence of thermal processing on the structural characteristics, and binding capacity of three core antigenic epitopes were studied. The results demonstrated that boiling, glycation and frying induced the down-regulation of the allergenicity of Ara h 2 in Balb/c mice, the collapse of its tertiary/secondary structure, and a reduction in the core epitope binding capacity; roasting showed a comparable allergenicity and the weakest inhibitory effect on core epitope binding capacity. These results indicate that thermal processing causes alteration of the protein structure and core epitopes of Ara h 2, and may affect its allergenicity.
authors.affiliation: Shanghai Key Laboratory of Bio-Energy Crops, School of Life Sciences, Shanghai University, Shanghai, PR China.
authors.forename: Wenju
authors.initials: W
authors.lastname: Zhang
authors.affiliation: Shanghai Key Laboratory of Bio-Energy Crops, School of Life Sciences, Shanghai University, Shanghai, PR China.
authors.forename: Qingqing
authors.initials: Q
authors.lastname: Zhu
authors.affiliation: Shanghai Key Laboratory of Bio-Energy Crops, School of Life Sciences, Shanghai University, Shanghai, PR China.
authors.forename: Tong
authors.initials: T
authors.lastname: Zhang
authors.affiliation: Shanghai Key Laboratory of Bio-Energy Crops, School of Life Sciences, Shanghai University, Shanghai, PR China; Shanghai Genechem Co., Ltd., Shanghai, PR China.
authors.forename: Qin
authors.initials: Q
authors.lastname: Cai
authors.affiliation: Shanghai Key Laboratory of Bio-Energy Crops, School of Life Sciences, Shanghai University, Shanghai, PR China. Electronic address: chenqincc@staff.shu.edu.cn.
authors.forename: Qin
authors.initials: Q
authors.lastname: Chen
mesh_terms: D055516:2S Albumins, Plant / Q000737:chemistry* / Q000276:immunology; D000485:Allergens / Q000737:chemistry* / Q000276:immunology; D000818:Animals; D000906:Antibodies / Q000737:chemistry; D052179:Antigens, Plant / Q000737:chemistry* / Q000276:immunology; D010367:Arachis / Q000737:chemistry*; D002942:Circular Dichroism; D015536:Down-Regulation; D000939:Epitopes / Q000737:chemistry; D005260:Female; D005511:Food Handling / Q000379:methods; D006023:Glycoproteins / Q000737:chemistry* / Q000276:immunology; D006031:Glycosylation; D006358:Hot Temperature; D007073:Immunoglobulin E / Q000276:immunology; D051379:Mice; D008807:Mice, Inbred BALB C; D021183:Peanut Hypersensitivity / Q000276:immunology; D010936:Plant Extracts / Q000276:immunology; D010940:Plant Proteins / Q000737:chemistry* / Q000276:immunology; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013056:Spectrophotometry, Ultraviolet
chemical_list: D055516:2S Albumins, Plant; D000485:Allergens; D000906:Antibodies; D052179:Antigens, Plant; C500890:Ara h 2 allergen, Arachis hypogaea; D000939:Epitopes; D006023:Glycoproteins; D010936:Plant Extracts; D010940:Plant Proteins; D007073:Immunoglobulin E
keywords: Allergenicity; Antigenic epitopes; Ara h 2; Peanut (Arachis hypogaea); Thermal processing