Journal article


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


Publication Details
Author(s): Meyer B, Baum F, Vollmer G, Pischetsrieder M
Publisher: American Chemical Society
Publication year: 2012
Volume: 60
Journal issue: 29
Pages range: 7306-7311
ISSN: 0021-8561

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.



How to cite
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://dx.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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