Caffeic acid-assisted cross-linking catalyzed by polyphenol oxidase decreases the allergenicity of ovalbumin in a Balb/c mouse model. (January 2018)

• Record Type: Journal Article
• Authors: Tong, Ping; Chen, Shuguang; Gao, Jinyan; Li, Xin; Wu, Zhihua; Yang, Anshu; Yuan, Juanli; Chen, Hongbing
• Is Part Of: Food and chemical toxicology. Volume 111(2018)
• Page Start: 275
• Page End: 283
• Publication Date: 2018-01
• Subjects: Ovalbumin -- Protein cross-linking -- Polyphenol oxidase -- Egg allergy; Toxicology -- Periodicals; Food poisoning -- Periodicals; Food Poisoning -- Periodicals; Toxicology -- Periodicals; Toxicologie -- Périodiques; Intoxications alimentaires -- Périodiques; Food poisoning; Toxicology; Periodicals; Electronic journals; 615.9
• DOI: 10.1016/j.fct.2017.11.026
• Languages: English
• ISSNs: 0278-6915

Abstract

Abstract: 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 allergenicity of OVA was tested in a Balb/c mouse model. Mice were orally sensitized with OVA or cross-linked OVA using cholera toxin as adjuvant. Clinical signs of allergy, specific antibody levels, serum histamine levels, mast cell protease-1 (mMCP-1) concentrations, morphological structure of duodenum, and cytokines were determined after mice were challenged with OVA or cross-linked OVA. Both OVA and cross-linked OVA induced allergic diarrhea in Balb/c mice, however, histological symptoms of small intestine were much milder in mice fed with cross-linked OVA than in those fed with OVA. A tendency toward decreased allergen-specific IgE, IgG, IgG1 and IgG2a levels, as well as serum histamine and mMCP-1 concentration were observed in cross-linked OVA group, accompanied by an inhibition of IL-4, IL-5, IL-13 and IFN-γ production in the stimulated spleen cell. It could be concluded that caffeic acid-assisted PPO-catalyzed cross-linking significantly reduced the potential allergenicity of OVA, but may not completely eliminate it. Highlights: Potential allergenicity of cross-linked ovalbumin (OVA) was assessed in a Balb/c mouse model. OVA was modified by polyphenol oxidase (PPO) with the assistant of caffeic acid (CA) to form intermolecular cross-links. The gastrointestinal digestibility of OVA was enhanced after it was cross-linked by PPO. CA-assisted PPO-catalyzed cross-linking was an effective method to significantly reduce the potential allergenicity of OVA.