Identification of glycated sites in ovalbumin under freeze-drying processing by liquid chromatography high-resolution mass spectrometry
Identification of glycated sites in ovalbumin under freeze-drying processing by liquid chromatography high-resolution mass spectrometry
复制标题
液相色谱高分辨质谱法鉴定冻干处理下卵清蛋白中的糖化位点
DOI：
10.1016/j.foodchem.2017.01.038
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发表时间：
2017-07-01
期刊：
影响因子：
8.8
通讯作者：
Wang, Hui
中科院分区：
文献类型：
--
作者：
Tu, Zong-cai;Zhong, Bi-zhen;Wang, Hui
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%. The glycated sites were located at the outer surface of the global protein. The unglycated sites were located at the outer surface of the hydrophobic pocket and in the six main strands of the beta-sheet. Therefore, the glycation reaction of the protein was occurred in the solvent accessible area. It was hypothesized that few changes occurred in the conformation to disturb the glycated sites under freeze-drying. In particular, the main strands of the beta-sheet of ovalbumin were more stable. Freeze-drying was a mild process and protected the conformation without extensive denaturation. (C) 2017 Published by Elsevier Ltd.
