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Download fileAnalysis of the Structure and Antigenicity in Ovalbumin Modified with Six Disaccharides Through Liquid Chromatography–High-Resolution Mass Spectrometry
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posted on 07.03.2022, 12:36 by Ya-ting Wang, Bi-zhen Zhong, Hui WangMelibiose, 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