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@article{faucris.122262624,
abstract = {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 β-lactoglobulin in processed milk. For this purpose, β-lactoglobulin, which had been heated with lactose under conditions to force nePTM formation (7 d/60 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 β-lactoglobulin were detected in different milk products. © 2013 American Chemical Society.},
author = {Meltretter, Jasmin and Wüst, Johannes and Pischetsrieder, Monika},
doi = {10.1021/jf401549j},
faupublication = {yes},
journal = {Journal of Agricultural and Food Chemistry},
keywords = {β-lactoglobulin; glycation; mass spectrometry; oxidation; processed milk; protein modification},
note = {UnivIS-Import:2015-03-09:Pub.2013.nat.dchph.llmch.compre},
pages = {6971-6981},
peerreviewed = {Yes},
title = {{Comprehensive} analysis of nonenzymatic post-translational beta-lactoglobulin modifications in processed milk by ultrahigh-performance liquid chromatography-tandem mass spectrometry},
url = {http://pubs.acs.org/articlesonrequest/AOR-gkwvWiD9kpAAJzuZtpnp},
volume = {61},
year = {2013}
}
@article{faucris.115023524,
abstract = {Thermal treatment of milk and milk products leads to protein oxidation, mainly the formation of methionine sulfoxide. Reactive oxygen species, responsible for the oxidation, can be generated by Maillard reaction, autoxidation of sugars, or lipid peroxidation. The present study investigated the influence of milk fat on methionine oxidation in milk. For this purpose, quantitative methionine sulfoxide profiling of all ten methionine residues of β-lactoglobulin, α-lactalbumin, and αs1-casein was carried out by ultrahigh-performance liquid chromatography–electrospray ionization tandem mass spectrometry with scheduled multiple reaction monitoring (UHPLC–ESI–MS/MS–sMRM). Analysis of defatted and regular raw milk samples after heating for up to 8 min at 120 °C and analysis of ultrahigh-temperature milk samples with 0.1%, 1.5%, and 3.5% fat revealed that methionine oxidation of the five residues of the whey proteins and of residues M 123, M 135, and M 196 of αs1-casein was not affected or even suppressed in the presence of milk fat. Only the oxidation of residues M 54 and M 60 of αs1-casein was promoted by lipids. In evaporated milk samples, formation of methionine sulfoxide was hardly influenced by the fat content of the samples. Thus, it can be concluded that lipid oxidation products are not the major cause of methionine oxidation in milk.},
author = {Wüst, Johannes and Pischetsrieder, Monika},
doi = {10.1039/c5fo01550b},
faupublication = {yes},
journal = {Food and Function},
pages = {2526-2536},
peerreviewed = {Yes},
title = {{Methionine} sulfoxide profiling of milk proteins to assess the influence of lipids on protein oxidation in milk},
volume = {7},
year = {2016}
}
@article{faucris.113836404,
abstract = {Site-specific relative quantification of β-lactoglobulin modifications in heated milk and dairy products was performed to determine their thermal and nonthermal origins and to evaluate marker candidates for milk processing. Therefore, formation kinetics of 19 different structures at 26 binding sites were analyzed by ultrahigh-performance liquid chromatography-tandem mass spectrometry with multiple reaction monitoring (UHPLC-MS/MS/MRM) after specific protein hydrolysis. The results indicate that (i) site-specific analysis of lactulosyllysine may be a more sensitive marker for mild heat treatment than its overall content; (ii) Nε-carboxymethyllysine, N-terminal ketoamide, and asparagine deamidation are of thermal origin and may be good markers for rather intensive heat treatment, whereas Nε-carboxyethyllysine reflects thermal and nonthermal processes; (iii) the relevance of methylglyoxal-derived arginine modifications is low compared to that of other modifications; (iv) oxidation of methionine and cysteine is a rather weak indicator of thermal impact; and (v) the tryptophan modifications formylkynurenine and kynurenine are of nonthermal origin and further degraded during processing.},
author = {Meltretter, Jasmin and Wüst, Johannes and Pischetsrieder, Monika},
doi = {10.1021/jf503664y},
faupublication = {yes},
journal = {Journal of Agricultural and Food Chemistry},
keywords = {heat marker; mass spectrometry; milk; protein modification; β-lactoglobulin},
note = {UnivIS-Import:2015-03-09:Pub.2014.nat.dchph.llmch.modifi},
pages = {10903-10915},
peerreviewed = {Yes},
title = {{Modified} peptides as indicators for thermal and nonthermal reactions in processed milk},
url = {http://pubs.acs.org/doi/full/10.1021/jf503664y},
volume = {62},
year = {2014}
}
@article{faucris.234386253,
abstract = {Nonenzymatic post-translational protein modifications (nePTMs) affect the nutritional, physiological, and technological properties of proteins in food and in vivo. In contrast to the usual targeted analyses, the present study determined nePTMs in processed milk in a truly untargeted proteomic approach. Thus, it was possible to determine to which extent known nePTM structures explain protein modifications in processed milk and to detect and identify novel products. The method combined ultrahigh-performance liquid chromatography coupled to electrospray ionization tandem mass spectrometry with bioinformatic data analysis by the software XCMS. The nePTMs detected by untargeted profiling of a β-lactoglobulin-lactose model were incorporated in a sensitive scheduled multiple reaction monitoring method to analyze these modifications in milk samples and to monitor their reaction kinetics during thermal treatment. Additionally, we identified the structures of unknown modifications. Lactosylation, carboxymethylation, formylation of lysine and N-terminus, glycation of arginine, oxidation of methionine, tryptophan, and cysteine, oxidative deamination of N-terminus, and deamidation of asparagine and glutamine were the most important reactions of β-lactoglobulin during milk processing. The isomerization of aspartic acid was observed for the first time in milk products, and N-terminal 4-imidazolidinone was identified as a novel nePTM.},
author = {Meltretter, Jasmin and Wüst, Johannes and Dittrich, Daniel and Lach, Johannes and Ludwig, Jonas and Eichler, Jutta and Pischetsrieder, Monika},
doi = {10.1021/acs.jproteome.9b00630},
faupublication = {yes},
journal = {Journal of Proteome Research},
keywords = {mass spectrometry; processed milk; protein modifications; untargeted profiling; β-lactoglobulin},
note = {CRIS-Team Scopus Importer:2020-02-18},
pages = {805-818},
peerreviewed = {Yes},
title = {{Untargeted} {Proteomics}-{Based} {Profiling} for the {Identification} of {Novel} {Processing}-{Induced} {Protein} {Modifications} in {Milk}},
volume = {19},
year = {2020}
}