Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 61, Issue 28, Pages 6971-6981Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf401549j
Keywords
protein modification; beta-lactoglobulin; glycation; oxidation; mass spectrometry; processed milk
Funding
- German Research Foundation (DFG)
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Nonenzymatic post-translational protein modifications (nePTMs) result in changes of the protein structure that may severely influence physiological and technological protein functions. In the present study, ultrahigh-performance liquid chromatography-electrospray ionization tandem mass spectrometry (UHPLC-ESI-MS/MS) was applied for the systematic identification and site-specific analysis of nePTMs of beta-lactoglobulin in processed milk. For this purpose, beta-lactoglobulin, which had been heated with lactose under conditions to force nePTM formation (7 d/60 degrees C), was screened for predicted modifications by using full scans and enhanced resolution scan experiments combined with enhanced product ion scans. Thus, the main glycation, glycoxidation, oxidation, and deamidation products of lysine, arginine, methionine, cysteine, tryptophan, and asparagine, as well as the N-terminus, were identified. Using these MS data, a very sensitive scheduled multiple reaction monitoring method suitable for the analysis of milk products was developed. Consequently, 14 different PTM structures on 25 binding sites of beta-lactoglobulin were detected in different milk products.
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