Lipid Hydroperoxide Induced Oxidation of Cysteine in Peptides

  • John W. Finley
  • Robert E. Lundin


Proteins may be exposed to a variety of oxidizing conditions during food processing and storage. Examples of deliberate oxidation are the addition of bromate, acetone peroxide or benzoyl peroxide to improve dough strength in the baking industry and the direct addition of hydrogen peroxide for bleaching or preservation elsewhere in the food industry (1). However, the most common oxidizing agents are lipid hydroperoxides. Urbanization of society has necessitated increased processing, shipping and storage of food products, all of which increase the likelihood of lipid hydroperoxide formation and possible development of off-flavors and odors. In protein foods containing polyunsaturated lipids, there is the additional risk of lipid hydroperoxide-induced oxidation of proteins and, more specifically, the sulfur amino acids of proteins. The oxidative changes in amino acids have been previously reviewed extensively (2,3,4,5,6). Significant nutritional losses have been reported in proteins which have been exposed to either hydrogen peroxide or oxidizing lipids (7,8).


Methyl Linoleate Lipid Hydroperoxide Protein Efficiency Ratio Sulfur Amino Acid Deuterium Oxide 
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Copyright information

© Springer Science+Business Media New York 1980

Authors and Affiliations

  • John W. Finley
    • 1
  • Robert E. Lundin
    • 1
  1. 1.Western Regional Research Center, Science and Education AdministrationUnited States Department of AgricultureBerkeleyUSA

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