LC-Orbitrap MS analysis of the glycation modification effects of ovalbumin during freeze-drying with three reducing sugar additives

文献类型： 外文期刊

第一作者： Chen, Yang

作者： Chen, Yang;Tu, Zong-cai;Wang, Hui;Liao, Zi-wei;Tu, Zong-cai;Liu, Guang-xian;Zhang, Lu;Liu, Guang-xian

作者机构：

关键词： Ovalbumin; Freeze-drying; Liquid chromatography high-resolution mass spectrometry; Glycated sites; Additives

期刊名称：FOOD CHEMISTRY （ 影响因子：7.514； 五年影响因子：7.516 ）

ISSN： 0308-8146

年卷期： 2018 年 268 卷

页码：

收录情况： SCI

摘要： In general, the reducing sugars were extensively utilized as additives to prevent denaturation and inactivation during the freeze-drying process. However, different additives have unequal protective effects on the protein conformation. To evaluate the mechanism of protection the protein structure using different additives in the freeze-drying process, the glycated sites and degree of substitution per peptide (DSP) of each site were investigated by LC-Orbitrap MS. We found that the ovalbumin that was supplemented with ribose and then lyophilized (R-oval) have the highest extent of glycation modification. K227 was the most reactive glycated site in R-Oval, with a DSP of 0.83. The ovalbumin that was supplemented with lactose and then lyophilized (L-Oval) have the lowest degree of glycation, and K227 did not undergo the glycation reaction. It was hypothesized that the order impact of different additives on protection of the protein conformation were lactose > galactose > ribose during the freeze-drying process.

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