Analysis of Bovine Kappa-Casein Glycomacropeptide by Liquid Chromatography-Tandem Mass Spectrometry

被引:10
|
作者
Qu, Yunyao [1 ,2 ]
Kim, Bum-Jin [2 ]
Koh, Jeewon [2 ]
Dallas, David C. [2 ]
机构
[1] Oregon State Univ, Dept Food Sci & Technol, Corvallis, OR 97331 USA
[2] Oregon State Univ, Coll Publ Hlth & Human Sci, Sch Biol & Populat Hlth Sci, Nutr Program, Corvallis, OR 97331 USA
关键词
LC-MS/MS; bovine casein; glycomacropeptide; top-down approach; MILK; GLYCOSYLATION; PHOSPHORYLATION; PROTEINS; CELLS;
D O I
10.3390/foods10092028
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Caseinomacropeptide (CMP) is released from bovine kappa-casein after rennet treatment and is one of the major peptides in whey protein isolate. CMP has in vitro anti-inflammatory and antibacterial activities. CMP has two major amino acid sequences with different modifications, including glycosylation, phosphorylation and oxidation. However, no previous work has provided a comprehensive profile of intact CMP. Full characterization of CMP composition and structure is essential to understand the bioactivity of CMP. In this study, we developed a top-down glycopeptidomics-based analytical method to profile CMP and CMP-derived peptides using Orbitrap mass spectrometry combined with nano-liquid chromatography with electron-transfer/higher-energy collision dissociation. The liquid chromatography-tandem mass spectrometry (LC-MS/MS) spectra of CMPs were annotated to confirm peptide sequence, glycan composition and other post-translational modifications using automatic data processing. Fifty-one intact CMPs and 159 CMP-derived peptides were identified in four samples (one CMP standard, two commercial CMP products and one whey protein isolate). Overall, this novel approach provides comprehensive characterization of CMP and CMP-derived peptides and glycopeptides, and it can be applied in future studies of product quality, digestive survival and bioactivity.
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页数:12
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