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Kanner, J., Department of Nutrition and Food Science, Massachusetts Institute of Technology, Cambridge, MA 02139, United States, Department of Food Technology, Agricultural Research Organization, Volcani Center, Bet Dagan, 50-200, Israel
Karel, M., Department of Nutrition and Food Science, Massachusetts Institute of Technology, Cambridge, MA 02139, United States
Lysozyme and peroxidizing methyl linoleate were allowed to react at 37°C in a freeze-dried model system adjusted to controlled water activities. Changes in solubility, fluorescence, enzymatic activity, and gel electrophoresis patterns of the protein fraction were studied and compared with changes in lysozyme irradiated with γ rays in the absence of linoleate. Reactions with peroxidizing linoleate were found to produce lysozyme dimers and higher polymers. The polymerization was due to covalent bonds. The degree of cross-linking, protein insolubilization, and loss of enzyme activity increased with increasing water activity.
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Changes in lysozyme due to reactions with peroxidizing methyl linoleate in a dehydreated model system
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Kanner, J., Department of Nutrition and Food Science, Massachusetts Institute of Technology, Cambridge, MA 02139, United States, Department of Food Technology, Agricultural Research Organization, Volcani Center, Bet Dagan, 50-200, Israel
Karel, M., Department of Nutrition and Food Science, Massachusetts Institute of Technology, Cambridge, MA 02139, United States
Changes in lysozyme due to reactions with peroxidizing methyl linoleate in a dehydreated model system
Lysozyme and peroxidizing methyl linoleate were allowed to react at 37°C in a freeze-dried model system adjusted to controlled water activities. Changes in solubility, fluorescence, enzymatic activity, and gel electrophoresis patterns of the protein fraction were studied and compared with changes in lysozyme irradiated with γ rays in the absence of linoleate. Reactions with peroxidizing linoleate were found to produce lysozyme dimers and higher polymers. The polymerization was due to covalent bonds. The degree of cross-linking, protein insolubilization, and loss of enzyme activity increased with increasing water activity.
Scientific Publication
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