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Changes in lysozyme due to reactions with peroxidizing methyl linoleate in a dehydreated model system
Year:
1976
Authors :
Kanner, Joseph
;
.
Volume :
24
Co-Authors:
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
Facilitators :
From page:
468
To page:
472
(
Total pages:
5
)
Abstract:
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.
Note:
Related Files :
chemistry
Electrophoresis, Polyacrylamide Gel
freeze drying
Linoleic Acids
lysozyme
metabolism
polyacrylamide gel electrophoresis
protein binding
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More details
DOI :
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
28525
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:39
Scientific Publication
Changes in lysozyme due to reactions with peroxidizing methyl linoleate in a dehydreated model system
24
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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