Analysis of the Structure and Antigenicity in Ovalbumin Modified with Six Disaccharides Through Liquid Chromatography–High-Resolution Mass Spectrometry
journal contributionposted on 07.03.2022, 12:36 by Ya-ting Wang, Bi-zhen Zhong, Hui Wang
Melibiose, cellobiose, maltose, lactose, turanose, and isomaltulose were selected to be glycated with OVA. The number of free amino groups of OVA modified with different disaccharides decreased, and the secondary and tertiary structures of the modified OVA also changed greatly. Moreover, the glycation sites detected by HPLC–HCD–MS/MS were all on the sensitized epitopes of OVA, which reduced the binding ability of IgG and IgE of glycated OVA. In addition, the glycation sites with the highest DSP in different samples were located in the irregular coil region of OVA. Among the six disaccharides, the glycation reaction between melibiose and OVA was the most obvious. Through the analysis of disaccharide configuration, it was found that the glycation efficiency of the reducing disaccharide linked by a 1 → 6 glycoside bond was higher than that by a 1 → 4 glycoside bond, and reducing sugar with β type was better than that with α type. These findings would provide a theoretical reference for the use of different sugars in food production.
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irregular coil regionfree amino groupsfindings would providereducing disaccharide linkeddifferent disaccharides decreasedglycation sites detectedglycation sitessix disaccharidesreducing sugardisaccharide configurationdifferent sugarsdifferent samplesglycation reactionglycation efficiencyβ typeα typetheoretical referencetertiary structuressensitized epitopesovalbumin modifiedhighest dspfood productionbinding ability