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Identification and quantification of the phosphorylated ovalbumin by high resolution mass spectrometry under dry-heating treatment

文献类型： 外文期刊

作者： Wang, Hui 1 ; Tu, Zong-cai 1 ; Liu, Guang-xian 2 ; Zhang, Lu 2 ; Chen, Yuan 2 ;

作者机构： 1.Nanchang Univ, State Key Lab Food Sci & Technol, Nanchang 330047, Jiangxi, Peoples R China

2.Jiangxi Normal Univ, Coll Life Sci, Nanchang 330022, Peoples R China

3.Jiangxi Acad Agr Sci, Nanchang 330200, Peoples R China

关键词： Ovalbumin;Phosphorylation;Mass spectrometry;Dry-heating treatment;Pepsin

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

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收录情况： SCI

摘要： The specific phosphorylation sites and degree of phosphorylation (DP) at each site are directly related to protein's structure and functional properties. Thus, characterizing the introduced phosphate groups is of great importance. This study was to monitor the phosphorylation sites, DP and the number of phosphorylation sites in P-Oval achieved by dry heating in the presence of pyrophosphate for 1, 2 and 5 days by using Fourier transform ion cyclotron mass spectrometry (FTICR MS). Two phosphorylation sites were found in natural ovalbumin, but the number of phosphorylation sites increased to 8, 8 and 10 after dry-heating phosphorylation for 1, 2 and 5 days, respectively. In addition, dual-phosphorylated peptides were detected for samples without extensive heating. The phosphorylation sites were found to be mainly on Ser residues, which could be the preferred phosphorylation site for dry heating in the presence of pyrophosphate. (C) 2016 Elsevier Ltd. All rights reserved.

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