Characterization of bison (Bison bison) myoglobin.

Area of Science:

• Food Science
• Biochemistry
• Animal Science

Background:

• Bison meat is a popular alternative to beef in North America.
• Previous studies suggest bison meat discolors faster than beef, but the molecular reasons are unclear.

Purpose of the Study:

• To investigate the molecular basis of bison meat discoloration.
• To compare the redox stability, thermostability, and primary structure of bison myoglobin (Mb) with beef Mb.

Main Methods:

• Analysis of autoxidation, lipid oxidation-induced oxidation, and thermostability of purified bison and beef myoglobins.
• Determination of bison Mb molecular mass using Matrix Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry.
• Determination of bison Mb amino acid sequence using Edman degradation.

Main Results:

• Bison and beef myoglobins exhibited similar behavior in autoxidation, lipid oxidation-induced oxidation, and thermostability.
• The molecular mass of bison Mb was determined to be 16,949 Da.
• Bison Mb primary structure showed 100% similarity to beef and yak myoglobins, but differed from other ruminant myoglobins.

Conclusions:

• The primary structure and biochemical properties of bison Mb are similar to beef Mb.
• The observed rapid discoloration of bison meat cannot be attributed to the biochemistry of bison myoglobin.