Species-specific effects on non-enzymatic metmyoglobin reduction in vitro

Our objectives were to determine the non-enzymatic metmyoglobin reduction properties of bovine, porcine, and equine myoglobins and to characterize the effects of pre-incubation of 4-hydroxy-2-nonenal (HNE) with myoglobins on non-enzymatic metmyoglobin reduction in vitro. Purified bovine, porcine, an...

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Bibliographic Details
Published in:Meat science 2015-07, Vol.105, p.108-113
Main Authors: Elroy, N.N., Rogers, J., Mafi, G.G., VanOverbeke, D.L., Hartson, S.D., Ramanathan, R.
Format: Article
Language:English
Subjects:
Aldehydes - pharmacology
Animals
Cattle
Cross-Linking Reagents - pharmacology
Dietary Proteins - chemistry
Dietary Proteins - isolation & purification
Dietary Proteins - metabolism
Electron Transport - drug effects
Horses
Hydrogen-Ion Concentration
Kinetics
Lipid oxidation
Lipid Peroxidation
Mass spectrometry
Meat color
Metmyoglobin - chemistry
Metmyoglobin - isolation & purification
Metmyoglobin - metabolism
Metmyoglobin reduction
Models, Molecular
Molecular Weight
Myoglobin
Oxidation-Reduction
Pigments, Biological - chemistry
Pigments, Biological - isolation & purification
Pigments, Biological - metabolism
Species Specificity
Spectrometry, Mass, Electrospray Ionization
Sus scrofa
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Summary:Our objectives were to determine the non-enzymatic metmyoglobin reduction properties of bovine, porcine, and equine myoglobins and to characterize the effects of pre-incubation of 4-hydroxy-2-nonenal (HNE) with myoglobins on non-enzymatic metmyoglobin reduction in vitro. Purified bovine, porcine, and equine metmyoglobins (0.05mM) were reduced at pH5.6 and 7.4 in the presence or absence of HNE. Rates of metmyoglobin reduction were monitored by spectrophotometry, and myoglobin adducts were characterized by high-resolution mass-spectrometry. Results showed that the species origins of individual myoglobins determined rates of non-enzymatic reduction (beef>equine>pork; P
ISSN:0309-1740
1873-4138
DOI:10.1016/j.meatsci.2015.03.010