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Oxymyoglobin oxidation and membranal lipid peroxidation initiated by iron redox cycle
Year:
2001
Authors :
Kanner, Joseph
;
.
Volume :
49
Co-Authors:
Gorelik, S., Department of Food Science, Institute for Technology and Storage of Agricultural Products, Agricultural Research Organization, P.O. Box 6, Bet Dagan 50250, Israel
Kanner, J., Department of Food Science, Institute for Technology and Storage of Agricultural Products, Agricultural Research Organization, P.O. Box 6, Bet Dagan 50250, Israel
Facilitators :
From page:
5939
To page:
5944
(
Total pages:
6
)
Abstract:
Oxymyoglobin is the main pigment in muscle tissues, responsible for the bright red color of fresh meat. Oxidation of the heme iron from the ferrous to the ferric metmyoglobin produces the brownish color that consumers find undesirable in fresh meat. The aim of this study was to elucidate the mechanism of oxymyoglobin oxidation in muscle tissues by using a model system containing oxymyoglobin and muscle membranes oxidized by an iron redox cycle. Oxidation of oxymyoglobin was determined from the decrease in absorption of the solution measured by a spectrophotometer at 582 nm. Lipid peroxidation was determined by accumulation of TBARS and conjugated dienes. The higher rates of oxidation of oxymyoglobin (20 μM) and lipid oxidation were achieved by using ferric iron and ascorbic acid at concentrations of 50 and 200 μM, respectively. Increasing the concentration of ascorbic acid to 2000 μM switched its effect to antioxidative. Increasing the concentration of oxymyoglobin from 20 to 80 μM inhibited lipid peroxidation by > 90% and partially prevented oxymyoglobin oxidation.
Note:
Related Files :
Animal
cattle
chemistry
iron
lipid peroxidation
Lipids
metabolism
myoglobin
oxidation
reaction analysis
unclassified drug
Show More
Related Content
More details
DOI :
10.1021/jf0104578
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
23591
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:00
Scientific Publication
Oxymyoglobin oxidation and membranal lipid peroxidation initiated by iron redox cycle
49
Gorelik, S., Department of Food Science, Institute for Technology and Storage of Agricultural Products, Agricultural Research Organization, P.O. Box 6, Bet Dagan 50250, Israel
Kanner, J., Department of Food Science, Institute for Technology and Storage of Agricultural Products, Agricultural Research Organization, P.O. Box 6, Bet Dagan 50250, Israel
Oxymyoglobin oxidation and membranal lipid peroxidation initiated by iron redox cycle
Oxymyoglobin is the main pigment in muscle tissues, responsible for the bright red color of fresh meat. Oxidation of the heme iron from the ferrous to the ferric metmyoglobin produces the brownish color that consumers find undesirable in fresh meat. The aim of this study was to elucidate the mechanism of oxymyoglobin oxidation in muscle tissues by using a model system containing oxymyoglobin and muscle membranes oxidized by an iron redox cycle. Oxidation of oxymyoglobin was determined from the decrease in absorption of the solution measured by a spectrophotometer at 582 nm. Lipid peroxidation was determined by accumulation of TBARS and conjugated dienes. The higher rates of oxidation of oxymyoglobin (20 μM) and lipid oxidation were achieved by using ferric iron and ascorbic acid at concentrations of 50 and 200 μM, respectively. Increasing the concentration of ascorbic acid to 2000 μM switched its effect to antioxidative. Increasing the concentration of oxymyoglobin from 20 to 80 μM inhibited lipid peroxidation by > 90% and partially prevented oxymyoglobin oxidation.
Scientific Publication
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