Effects of covalent conjugation with quercetin and its glycosides on the structure and allergenicity of Bra c p from bee pollen. (16th April 2023)

• Record Type: Journal Article
• Authors: Zhou, Enning; Xue, Xiaofeng; Xu, Haoxie; Zhao, Liuwei; Wu, Liming; Li, Qiangqiang
• Is Part Of: Food chemistry. Volume 406(2023)
• Publication Date: 2023-04-16
• Subjects: Bee pollen allergen -- Profilin -- Quercetin -- Covalent conjunction -- Structural changes -- Allergenicity; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2022.135075
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Quercetin had excellent non-covalent and covalent binding ability with Bra c p. Structural property of Bra c p was changed after covalent binding with quercetin. Antioxidant ability of Bra c p-quercetin covalent polymer was improved. The IgE-binding capacity of Bra c p-quercetin covalent polymer was decreased. Abstract: Profilin family members are potential pan-allergens in foods, presenting public health hazards. However, studies on the allergenicity modification of profilin allergens are limited. Herein, quercetin and its glycosides (isoquercitrin and rutin) were applied to modify the allergenicity of a profilin allergen (Bra c p) from Brassica campestris bee pollen. Results showed that only quercetin can be closely covalently bound to Bra c p among the three, and the binding site was located at the Cys98 residue. After covalently conjunction, the relative content of α-helix structure in Bra c p was reduced by 40.05%, while random coil was increased by 42.89%; moreover, the Tyr and Phe residues in Bra c p were masked. These structural changes could alter the conformational antigenic epitopes of Bra c p, resulting in its allergenicity reduction. Our findings might provide a technical foundation for reducing the allergenicity of bee pollen and foods containing profilin family allergens.