Myoglobin from common pheasant (Phasianus colchicus L.): Purification and primary structure characterization

Myoglobin (Mb) is a monomeric hemoprotein involved in dioxygen storage and transport in skeletal muscles and heart. Mb, containing the heme pigment, is present in large amount in meat, thus influencing meat color and consumer choice. Here, the primary structure of Mb isolated from muscle of Phasianus colchicus L. was determined by using a comparative peptide mapping approach based on MALDI-TOF mass spectrometry. This strategy allowed the determination of common pheasant Mb primary sequence, which resulted identical to the chicken Mb, as also confirmed by intact molecular mass determination by ESI/Q-TOF mass spectrometry. Indeed, the accurate molecular mass (17,290.50 Da) of common pheasant Mb was found to be in good agreement with that of chicken Mb (17,290.86 Da). Finally, the 3D model of common pheasant Mb was predicted by homology modeling. Overall, in this study we confirmed that chicken, turkey and common pheasant, belonging to the Galliformes order, share the same Mb sequence. Practical applications: Considering the economic importance of game meat consumption, our result may be interesting for meat industry, providing useful information for the determination of species-specific differences in color and color stability compared to other poultry species.