Characterization of bison (Bison bison) myoglobin

P. Joseph, S. P. Suman, S. Li, C. M. Beach, Laurey A Steinke, M. Fontaine

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Bison is an alternate meat species gaining increased popularity in North America. Although previous investigations reported that bison meat discolors faster than beef, the molecular basis of this observation has not been investigated. Therefore, the objective of the present study was to determine the redox stability, thermostability, and primary structure of bison myoglobin (Mb), in comparison with beef Mb. Purified bison and beef myoglobins were analyzed for autoxidation, lipid oxidation-induced oxidation, and thermostability. Matrix Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry was utilized for determining the exact molecular mass of bison Mb, whereas Edman degradation was employed to determine the amino acid sequence. Bison and beef myoglobins behaved similarly in autoxidation, lipid oxidation-induced oxidation, and thermostability. The observed molecular mass of bison and beef myoglobins was 16,949 Da, and the primary structure of bison Mb shared 100% similarity with beef and yak myoglobins. Noticeably, the amino acid sequence of bison Mb was different from other ruminant myoglobins, such as water-buffalo, sheep, goat, and red-deer. The present study is the first to report the primary structure of bison Mb. Same primary structure and similar biochemical attributes of bison and beef myoglobins suggested that the observed rapid discoloration in bison meat could not be attributed to biochemistry of bison Mb.

Original languageEnglish (US)
Pages (from-to)71-78
Number of pages8
JournalMeat Science
Volume84
Issue number1
DOIs
StatePublished - Jan 1 2010

Fingerprint

Bison
bison
myoglobin
Myoglobin
beef
thermal stability
buffalo meat
Meat
autoxidation
Bison bison
Amino Acid Sequence
lipid peroxidation
meat substitutes
amino acid sequences
oxidation
molecular weight
Lipids
yaks
Deer
matrix-assisted laser desorption-ionization mass spectrometry

Keywords

  • Bison
  • Edman degradation
  • Mass spectrometry
  • Myoglobin
  • Primary structure
  • Redox stability
  • Thermostability

ASJC Scopus subject areas

  • Food Science

Cite this

Joseph, P., Suman, S. P., Li, S., Beach, C. M., Steinke, L. A., & Fontaine, M. (2010). Characterization of bison (Bison bison) myoglobin. Meat Science, 84(1), 71-78. https://doi.org/10.1016/j.meatsci.2009.08.014

Characterization of bison (Bison bison) myoglobin. / Joseph, P.; Suman, S. P.; Li, S.; Beach, C. M.; Steinke, Laurey A; Fontaine, M.

In: Meat Science, Vol. 84, No. 1, 01.01.2010, p. 71-78.

Research output: Contribution to journalArticle

Joseph, P, Suman, SP, Li, S, Beach, CM, Steinke, LA & Fontaine, M 2010, 'Characterization of bison (Bison bison) myoglobin', Meat Science, vol. 84, no. 1, pp. 71-78. https://doi.org/10.1016/j.meatsci.2009.08.014
Joseph, P. ; Suman, S. P. ; Li, S. ; Beach, C. M. ; Steinke, Laurey A ; Fontaine, M. / Characterization of bison (Bison bison) myoglobin. In: Meat Science. 2010 ; Vol. 84, No. 1. pp. 71-78.
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