Related Experiment Videos
Deoxyhemoglobin-mediated lipid oxidation in washed fish muscle
Mark P Richards1, Henrik Østdal, Henrik J Andersen
1Muscle Biology and Meat Science Laboratory, University of Wisconsin-Madison, Madison, WI 53706-1284, USA. mprichards@facstaff.wisc.edu
Journal of Agricultural and Food Chemistry
|February 21, 2002
Summary
Deoxyhemoglobin, the deoxygenated form of hemoglobin, significantly accelerates lipid oxidation in fish muscle. This finding highlights the importance of hemoglobin
Area of Science:
- Food Science
- Biochemistry
- Fish Muscle Quality
Background:
- Lipid oxidation is a major cause of fish spoilage.
- Hemoglobin's role in fish muscle oxidation is not fully understood.
- Trout hemoglobins exhibit different properties.
Purpose of the Study:
- To compare the pro-oxidative activity of different trout hemoglobin types.
- To investigate the impact of oxygenation state on hemoglobin's pro-oxidative effects.
- To understand lipid oxidation in postmortem fish muscle.
Main Methods:
- Utilized a washed cod muscle model system.
- Compared anodic and cathodic trout hemoglobins.
- Measured thiobarbituric acid reactive substances (TBARS) and redness (a value).
- Assessed lipid hydroperoxide formation.
Main Results:
- Anodic hemoglobins initiated lipid oxidation more rapidly than cathodic hemoglobins.
- Deoxyhemoglobin showed greater pro-oxidative activity than oxyhemoglobin.
- Reduced redness (a value) indicated faster oxidation with anodic hemoglobins.
- Adenosine triphosphate enhanced oxidation by reducing hemoglobin oxygenation.
Conclusions:
- Deoxyhemoglobin is more pro-oxidative than oxyhemoglobin in fish muscle.
- Hemoglobin's oxygenation state is critical for lipid oxidation.
- Findings are relevant to understanding fish spoilage mechanisms.