Myoglobins: the link between discoloration and lipid oxidation in muscle and meat

Quimica nova

Skibsted, Leif H.¹  Møller, Jens K. S.² 

[1] Royal Veterinary and Agricultural University, Frederiksberg, Denmark;Universidade Estadual de Campinas, Campinas, Brazil

关键词: myoglobin complexes;    heme iron;    oxidative processes.;   

DOI  :  10.1590/S0100-40422006000600024

学科分类：化学（综合）

来源: Sociedade Brasileira de Quimica

【 摘 要 】

Aerobic metabolism changes rapidly to glycolysis post-mortem resulting in a pH-decrease during the transformation of musclein to meat affecting ligand binding and redox potential of the heme iron in myoglobin, the meat pigment. The "inorganicchemistry" of meat involves (i) redox-cycling between iron(II), iron(III), and iron(IV)/protein radicals; (ii) ligand exchange processes;and (iii) spin-equilibra with a change in coordination number for the heme iron. In addition to the function of myoglobin foroxygen storage, new physiological roles of myoglobin are currently being discovered, which notably find close parallels in theprocesses in fresh meat and nitrite-cured meat products. Myoglobin may be characterized as a bioreactor for small molecules likeO2, NO, CO, CO2,H2O, and HNO with importance in bio-regulation and in protection against oxidative stress in vivo otherwiseaffecting lipids in membranes. Many of these processes may be recognised as colour changes in fresh meat and cured meat productsunder different atmospheric conditions, and could also be instructive for teaching purposes.

【 授权许可】

CC BY