Abstract
ABSTRACTProteins in contact with peroxidizing lipids undergo various degradative reactions, including polymerization. Reaction of lysozyme with peroxidizing methyl linoleate at a water activity of 0.75 causes polymerization and partial denaturation of the protein. Polymerization occurs by addition of monomers, both native and denatured. The partial denaturation is probably due to the opening of a disulfide bond and occurs independently of polymerization. This denatured fraction as well as dimer and trimer fractions was isolated and characterized with respect to enzymatic activity, tryptophan content, molecular weight, hydrodynamic volume, and circular dichroism.
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