Journal
FOOD CHEMISTRY
Volume 229, Issue -, Pages 417-424Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2017.02.102
Keywords
Aldehyde reactive probe; Glyoxal; Infant formula; Milk proteomics; Oxidation; Protein carbonylation
Funding
- Deutsche Forschungsgemeinschaft [HO2222/7-1]
- European Fund for Regional Structure Development (EFRE) [100055720, 100092961, 100146238]
- European Fund for Regional Structure Development (EFRE, European Union and Free State Saxony)
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During thermal treatment of milk, proteins are oxidized, which may reduce the nutritional value of milk, abolish protein functions supporting human health, especially important for newborns, and yield potentially harmful products. The side chains of several amino acids can be oxidized to reactive carbonyls, which are often used to monitor oxidative stress in organisms. Here we mapped protein carbonylation sites in raw milk and different brands of pasteurized, ultra high temperature (UHT) treated milk, and infant formulas (IFs) after digesting the precipitated proteins with trypsin. Reactive carbonyls were derivatized with O-(biotinylcarbazoylmethyl)hydroxylamine to enrich the modified peptides by avidin-biotin affinity chromatography and analyze them by nanoRP-UPLC-ESI-MS. Overall, 53 unique carbonylated peptides (37 carbonylation sites, 15 proteins) were identified. Most carbonyls were derived from dicarbonyls (mainly glyoxal). The number of carbonylation sites increased with the harsher processing from raw milk (4) to pasteurized (16) and UHT milk (16) and to IF (24). (C) 2017 Elsevier Ltd. All rights reserved.
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