Journal
PROTEOMICS
Volume 11, Issue 3, Pages 420-428Publisher
WILEY-BLACKWELL
DOI: 10.1002/pmic.201000233
Keywords
2-DE; Advanced glycation end-products; Glycoproteomics; Milk proteome; N-epsilon-carboxymethyllysine; Protein-specific modification
Funding
- Deutsche Forschungsgemeinschaft (DFG)
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Milk processing leads to severe protein damage caused by the formation of nonenzymatic posttranslational modifications (nePTMs), such as glycation and glycoxidation. As a result, the technological and nutritional function of milk proteins can be critically altered. The present study investigated the protein-specific distribution of the glycoxidation product N-epsilon-carboxymethyllysine (CML) in the proteome of processed milk. For this purpose, raw milk and heated milk were separated by 1-D or 2-DE. The distribution of CML in the milk proteome was examined by immunoblotting. The changes in the protein composition that occurred during heating were monitored by Coomassie staining. Relative modification rates were measured for the major milk protein fractions after 30 and 60 mm of heating at 120 degrees C and normalized to the content of the respective protein fraction in the samples. The highest glycoxidation rates were detected in the high molecular weight aggregates that are generated during heating. The casein fraction and the whey protein beta-lactoglobulin were affected in a similar manner. The relevance of the results for industrial milk processing was confirmed by analyzing several commercial milk products accordingly. The presented approach allows nonenzymatic posttranslational modification mapping of the entire milk proteome.
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