Analysis of the Structure and Antigenicity in Ovalbumin Modified with Six Disaccharides Through Liquid Chromatography-High-Resolution Mass Spectrometry.

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.

Investigation of the effect of oxidation on the structure of β-lactoglobulin by high resolution mass spectrometry.

In this work, high-resolution mass spectrometry was used to identify the oxidation sites and forms of β-lactoglobulin (β-Lg) induced by hydrogen peroxide with 1.5% concentration, and the influence of oxidation sites on the structure of β-Lg was discussed from the molecular level. Twelve kinds of oxidation products and 36 oxidation sites were identified, including sulfoxidation in sulfur-containing amino acid residue, hydroxylation in aromatic group residue, deamination in amino-containing amino acid etc.

Enzymolysis Reaction Kinetics and Liquid Chromatography High-Resolution Mass Spectrometry Analysis of Ovalbumin Glycated with Microwave Radiation.

Microwave radiation was adopted to accelerate glycation between ovalbumin (OVA) and d-glucose. We evaluated the digestibility of glycated OVA from the perspective of kinetics, using pepsin and trypsin as model enzymes. Hydrolysed protein concentrations, enzymolysis kinetics, and activation energy () were investigated.

Identification of glycated sites in ovalbumin under freeze-drying processing by liquid chromatography high-resolution mass spectrometry.

The glycation reaction between ovalbumin and d-glucose during freeze-drying was investigated and the mechanism of protection of the protein structure was studied, the precise glycated sites and degree of substitution per peptide (DSP) of each site were determined using liquid chromatography high-resolution mass spectrometry. It was found that lysine residues are the main glycated sites under freeze-drying. K62 and K264 were the most reactive glycated sites in lyophilized ovalbumin, with a DSP close to 80%.