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Lipids
Kanner, J., Division of Food Technology, Institute for Technology and Storage of Agricultural Products, Agricultural Research Organization, Volcani Center, PO Box 6, Bet Dagar, 50-100, Israel
Ben-Gera, I., Division of Food Technology, Institute for Technology and Storage of Agricultural Products, Agricultural Research Organization, Volcani Center, PO Box 6, Bet Dagar, 50-100, Israel
Berman, S., Division of Food Technology, Institute for Technology and Storage of Agricultural Products, Agricultural Research Organization, Volcani Center, PO Box 6, Bet Dagar, 50-100, Israel
The effect of nitric-oxide myoglobin (MbNO) on lipid oxidation was studied in linoleate and β-carotene-linoleate aqueous model systems and compared with that of metmyoglobin (MMb) and oxymyoglobin (MbO2) in short- and long-term reactions. While MMb and MbO2 had a clear prooxidative effect, MbNO, under the same conditions, acted as an antioxidant. The specific antioxidative activity of MbNO was maintained even in the presence of prooxidants such as hemeproteins. The significance of the conversion of MbO2 and MMb into an antioxidant during the curing process is discussed. © 1980 American Oil Chemists' Society.
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תנאי שימוש
Nitric-oxide myoglobin as an inhibitor of lipid oxidation
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Kanner, J., Division of Food Technology, Institute for Technology and Storage of Agricultural Products, Agricultural Research Organization, Volcani Center, PO Box 6, Bet Dagar, 50-100, Israel
Ben-Gera, I., Division of Food Technology, Institute for Technology and Storage of Agricultural Products, Agricultural Research Organization, Volcani Center, PO Box 6, Bet Dagar, 50-100, Israel
Berman, S., Division of Food Technology, Institute for Technology and Storage of Agricultural Products, Agricultural Research Organization, Volcani Center, PO Box 6, Bet Dagar, 50-100, Israel
Nitric-oxide myoglobin as an inhibitor of lipid oxidation
The effect of nitric-oxide myoglobin (MbNO) on lipid oxidation was studied in linoleate and β-carotene-linoleate aqueous model systems and compared with that of metmyoglobin (MMb) and oxymyoglobin (MbO2) in short- and long-term reactions. While MMb and MbO2 had a clear prooxidative effect, MbNO, under the same conditions, acted as an antioxidant. The specific antioxidative activity of MbNO was maintained even in the presence of prooxidants such as hemeproteins. The significance of the conversion of MbO2 and MMb into an antioxidant during the curing process is discussed. © 1980 American Oil Chemists' Society.
Scientific Publication
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