Distribution of protein oxidation products in the proteome of thermally processed milk

Meyer B, Baum F, Vollmer G, Pischetsrieder M (2012)


Publication Type: Journal article

Publication year: 2012

Journal

Publisher: American Chemical Society

Book Volume: 60

Pages Range: 7306-7311

Journal Issue: 29

URI: http://pubs.acs.org/articlesonrequest/AOR-sGNK96F3UuWpRtBJq3zu

DOI: 10.1021/jf301666r

Abstract

During thermal milk processing, severe oxidation can occur, which alters the technological and physiological properties of the milk proteins. Due to differences in composition and physicochemical properties, it can be expected that the particular milk proteins are differently affected by oxidative damage. Therefore, the protein-specific distribution of oxidation products in the heated milk proteome was investigated. Raw and heated milk samples were separated by one-dimensional gel electrophoresis. Protein oxidation was visualized by Western blot after derivatization of protein carbonyls with 2,4-dinitrophenylhydrazine. Thus, α-lactalbumin displayed enhanced oxidation compared to α-lactoglobulin, despite its lower concentration in milk. Highly selective oxidation was detected for a previously unassigned minor milk protein. The protein was identified by its peptide mass fingerprint as a variant of αS1-casein (αS1-casein*). Similar oxidation patterns were observed in several commercial milk products. © 2012 American Chemical Society.

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APA:

Meyer, B., Baum, F., Vollmer, G., & Pischetsrieder, M. (2012). Distribution of protein oxidation products in the proteome of thermally processed milk. Journal of Agricultural and Food Chemistry, 60(29), 7306-7311. https://doi.org/10.1021/jf301666r

MLA:

Meyer, Bianca, et al. "Distribution of protein oxidation products in the proteome of thermally processed milk." Journal of Agricultural and Food Chemistry 60.29 (2012): 7306-7311.

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