Temperature and pH Dependence of the Autoxidation Rate of Bovine, Ovine, Porcine, and Cervine Oxymyoglobin Isolated from Three Different Muscles-Longissimus dorsi, Gluteus medius, and Biceps femoris

Gutzke, Dean and Trout, Graham R. (2002) Temperature and pH Dependence of the Autoxidation Rate of Bovine, Ovine, Porcine, and Cervine Oxymyoglobin Isolated from Three Different Muscles-Longissimus dorsi, Gluteus medius, and Biceps femoris. Journal of Agricultural and Food Chemistry, 50 9: 2673-2678. doi:10.1021/jf0112769


Author Gutzke, Dean
Trout, Graham R.
Title Temperature and pH Dependence of the Autoxidation Rate of Bovine, Ovine, Porcine, and Cervine Oxymyoglobin Isolated from Three Different Muscles-Longissimus dorsi, Gluteus medius, and Biceps femoris
Formatted title
Temperature and pH Dependence of the Autoxidation Rate of Bovine, Ovine, Porcine, and Cervine Oxymyoglobin Isolated from Three Different Muscles - Longissimus dorsi, Gluteus medius, and Biceps femoris
Journal name Journal of Agricultural and Food Chemistry   Check publisher's open access policy
ISSN 0021-8561
Publication date 2002
Sub-type Article (original research)
DOI 10.1021/jf0112769
Volume 50
Issue 9
Start page 2673
End page 2678
Total pages 6
Place of publication United States
Publisher American Chemical Society
Language eng
Subject 03 Chemical Sciences
07 Agricultural and Veterinary Sciences
Formatted abstract
This study examined the temperature and pH dependence of the in vitro autoxidation rate of bovine, ovine, porcine, and cervine oxymyoglobin that had been isolated and purified from three muscles of different oxidative stability Longissimus dorsi, Gluteus medius, and Biceps femoris. To avoid obtaining unreliable estimates of autoxidation rate as has occurred in many previous studies, in this study, precautions were taken to eliminate the effects of freezing, chemical reduction with hydrosulfite, and contaminating metal ions on the reaction rate. When these precautions were taken, the rate constants for the different myoglobins studied were similar to each other but were 2−7-fold lower, and the Ea (activation energy) was 20−100% higher than that reported in most previous studies. The type of muscle the myoglobin was isolated from had no effect on the reaction rate or the Ea; however, the species did have a significant effect (p < 0.05) with porcine myoglobin having a 10% lower reaction rate and a 20% lower Ea than myoglobin from the other species. Increasing the reaction pH from 5.50 to 6.50 produced an exponential increase in reaction rate but only a small curvilinear change in Ea that had a maximum at pH 6.00.
Keyword Myoglobin
autoxidation
ovine
bovine
porcine
cervine
temperature dependence
muscle type
pH
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: School of Biomedical Sciences Publications
School of Chemistry and Molecular Biosciences
 
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Created: Thu, 20 Apr 2006, 20:02:16 EST