Formation, characterization, and antigenicity of lecithin-β-conglycinin complexes. (1st May 2023)

• Record Type: Journal Article
• Authors: Yang, Hui; Gao, Yaran; Sun, Shuyuan; Qu, Yezhi; Ji, Shuaiqi; Wu, Rina; Wu, Junrui
• Is Part Of: Food chemistry. Volume 407(2023)
• Publication Date: 2023-05-01
• Subjects: β-Conglycinin -- Lecithin -- Binding behavior -- Antigenicity -- Heat treatment; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2022.135178
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Quenching mechanism of lecithin to β-conglycinin belongs to static with high-affinity binding. The binding reaction was spontaneous and mainly driven by hydrogen bonds and van der Waals forces. The structure unfolded and more hydrophobic regions were exposed for complexes after heat treatment. The antigenicity of complexes was inhibited with increased temperature as some epitopes may be masked. Abstract: Lipid binding has been proposed to represent a functional property of many allergenic proteins. This study investigated the formation, characterization, and antigenicity of lecithin-β-conglycinin complexes. The results indicate that lecithin was combined with β-conglycinin via static quenching and primarily driven by hydrogen bonds and van der Waals forces. In addition, heat treatment reduced the antigenicity of complexes, as evidenced by changes in molecular weight and secondary and tertiary structures. It revealed that large aggregates developed and more hydrophobic regions were exposed for complexes after heat treatment, as well as a decrease in the β-sheet contents and an increase in the β-turn and random coil contents. Furthermore, the average particle size of the complexes increased with increased temperature treatment, and the morphology of the complexes exhibited an amorphous polymer. These findings shed light on the interaction between lecithin and β-conglycinin and help us understand the role of lecithin in allergic reactions.