Meyer B, Al-Diab D, Vollmer G, Pischetsrieder M (2011)
Publication Type: Journal article
Publication year: 2011
Publisher: Wiley-VCH Verlag
Book Volume: 11
Pages Range: 420-428
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 Ne-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 min of heating at 1201C 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 b-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.
APA:
Meyer, B., Al-Diab, D., Vollmer, G., & Pischetsrieder, M. (2011). Mapping the glycoxidation product Nepsilon-carboxymethyllysine in the milk proteome. Proteomics, 11, 420-428. https://dx.doi.org/10.1002/pmic.201000233
MLA:
Meyer, Bianca, et al. "Mapping the glycoxidation product Nepsilon-carboxymethyllysine in the milk proteome." Proteomics 11 (2011): 420-428.
BibTeX: Download