The chemistry of myoglobin and its reactions

The chemistry of myoglobin and its reactions

1981

REP.G0928

MYOGLOBIN is the main pigment of concern to meat scientists and to processors of beef, pork, lamb, poultry, and many types of fish. The form that this protein takes in these muscle foods is of prime importance in determining the color of the product, one of the main quality indices of importance to the consumer. Therefore, an understanding of the myoglobin molecule, its structure, and its reactivity is desirable in aiding the prediction and control of the color of all the products in which it is found. This review article will concentrate on the structure and chemistry of myoglobin. We shall note where hemoglobin differs from myoglobin in common color reactions; however, for most of the discussion, we will assume that common reactions are occurring with either protein. Our discussion will cover the following topics: the properties of the iron center in myoglobin; the most common iron-ligand complexes found in fresh, cooked, and cured meats; and how these derivatives are interconverted. We shall then examine the overall structure of this protein and how differences in the structure of myoglobin between species of animal can cause different sensitivities to conditions encountered during meat handling. Finally, we shall examine myoglobin as a part of the meat system and how the in-situ conditions can affect its color. Much of the data presented in this review have been obtained in our laboratory. For a more general review on myoglobin, we recommend that of Giddings (1977), who presents a comprehensive summary of the more important work done on myoglobin in recent years.

v.35(5):244-252, FOOD TECHNOLOGY

Research > Published Articles