Study on ovalbumin molecular properties changes in the process of glycation reaction

With egg white ovalbumin glycosylation reaction product as the research object,monitoring glycosylation reaction process, changes in the protein molecular characteristics. Experimental results showed that with prolongation of reaction time, ovalbumin and monosaccharide and polysaccharide of reaction product grafting degree increased gradually, and the same reaction time and reactions of monosaccharide graft copolymer was larger; glycosylated ovalbumin surface thiol relative content of 3 days before gradually increased, the 4 day reached maximum value, and the relative content of glycosylated ovalbumin surface thiol was always higher than that of ovalbumin. In 1-3 days,with the extension of reaction time, the hydrophobicity of the glycosylated albumin increased significantly, and the hydrophobicity of the 3 days later, the size of the large volume of the reaction system increased gradually with the increase of the reaction time, and the first 3 days with a large area of the rapid increase in particle number. Experimental results showed that, glycosylation could improve the hydrophobicity and molecular size of ovalbumin. Determined the secondary structure of ovalbumin before and after the glycosylation reaction, infrared spectroscopy and circular dichroism analysis showed that the glycosylation reaction to ovalbumin α-helix content decreases gradually; β-sheet was the β- turn content continues to increase; coil content with the wavy changes in reaction time, the greatest change in the β-sheet content.