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Meat science2015; 105; 108-113; doi: 10.1016/j.meatsci.2015.03.010

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

Abstract: 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 (0.05 mM) were reduced at pH 5.6 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<0.05). Irrespective of species, pre-incubation of HNE myoglobin decreased non-enzymatic metmyoglobin reduction compared with control at both pH 5.6 and 7.4 (P<0.05). Mass spectrometric analysis revealed adducts of HNE with bovine, porcine, and equine myoglobins. The results indicate that the amino acid composition and the covalent binding of HNE with myoglobin can significantly decrease the ability of heme to accept electrons.
Publication Date: 2015-03-19 PubMed ID: 25828165DOI: 10.1016/j.meatsci.2015.03.010Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The research examined the reduction properties of myoglobins in different species (bovine, porcine, and equine) and the effect of pre-incubation with 4-hydroxy-2-nonenal (HNE), concluding that species-specific myoglobins and the presence of HNE can significantly affect the reduction process.

Objectives and Methodology

  • The primary goals of the study were to observe the non-enzymatic metmyoglobin reduction attributes in bovine, porcine, and equine myoglobins, and priorly incubating these myoglobins with HNE and analyze its impact on the reduction procedure.
  • Purified metmyoglobins from these species were reduced at various pH conditions, and the rates of reduction were then observed through spectrophotometry.
  • After this, myoglobin adducts were identified using high-resolution mass-spectrometry.

Results

  • It was found that the reduction rate varied with the species origin of the myoglobins, with beef myoglobin showing the highest rate, followed by equine and then pork.
  • Interestingly, irrespective of the species, the presence of HNE myoglobin led to a decrease in non-enzymatic metmyoglobin reduction.
  • Mass spectrometric analysis revealed adducts of HNE with all three types of myoglobins.

Conclusions

  • The paper concludes that the rate of non-enzymatic metmyoglobin reduction is influenced by the species of origin of the myoglobin. The bovine myoglobin was found to have the highest reduction rate, followed by equine and porcine myoglobins.
  • Furthermore, pre-incubation with HNE consistently led to a reduction in the rate of non-enzymatic metmyoglobin reduction across all species.
  • This research suggests that the amino acid composition and covalent bonding of HNE with myoglobin can significantly reduce the heme’s electron-accepting ability.

Cite This Article

APA
Elroy NN, Rogers J, Mafi GG, VanOverbeke DL, Hartson SD, Ramanathan R. (2015). Species-specific effects on non-enzymatic metmyoglobin reduction in vitro. Meat Sci, 105, 108-113. https://doi.org/10.1016/j.meatsci.2015.03.010

Publication

ISSN: 1873-4138
NlmUniqueID: 101160862
Country: England
Language: English
Volume: 105
Pages: 108-113
PII: S0309-1740(15)00071-6

Researcher Affiliations

Elroy, N N
  • Department of Animal Science, Oklahoma State University, Stillwater, OK 74078, USA.
Rogers, J
  • Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
Mafi, G G
  • Department of Animal Science, Oklahoma State University, Stillwater, OK 74078, USA.
VanOverbeke, D L
  • Department of Animal Science, Oklahoma State University, Stillwater, OK 74078, USA.
Hartson, S D
  • Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
Ramanathan, R
  • Department of Animal Science, Oklahoma State University, Stillwater, OK 74078, USA. Electronic address: ranjith.ramanathan@okstate.edu.

MeSH Terms

  • 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 Peroxidation
  • Metmyoglobin / chemistry
  • Metmyoglobin / isolation & purification
  • Metmyoglobin / metabolism
  • Models, Molecular
  • Molecular Weight
  • Oxidation-Reduction
  • Pigments, Biological / chemistry
  • Pigments, Biological / isolation & purification
  • Pigments, Biological / metabolism
  • Species Specificity
  • Spectrometry, Mass, Electrospray Ionization
  • Sus scrofa

Citations

This article has been cited 2 times.
  1. Gan M, Shen L, Fan Y, Guo Z, Liu B, Chen L, Tang G, Jiang Y, Li X, Zhang S, Bai L, Zhu L. High Altitude Adaptability and Meat Quality in Tibetan Pigs: A Reference for Local Pork Processing and Genetic Improvement.. Animals (Basel) 2019 Dec 3;9(12).
    doi: 10.3390/ani9121080pubmed: 31817035google scholar: lookup
  2. López-Romero JC, Ayala-Zavala JF, Peña-Ramos EA, Hernández J, González-Ríos H. Antioxidant and antimicrobial activity of Agave angustifolia extract on overall quality and shelf life of pork patties stored under refrigeration.. J Food Sci Technol 2018 Nov;55(11):4413-4423.
    doi: 10.1007/s13197-018-3351-3pubmed: 30333637google scholar: lookup