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In living muscle, the concentration of metmyoglobin is vanishingly small, due to the presence of the enzyme metmyoglobin reductase, which, in the presence of the cofactor NADH and the coenzyme cytochrome b4 converts the Fe3+ in the haem prosthetic group of metmyoglobin back to the Fe2+ of normal myoglobin. In meat, which is dead muscle, the normal processes of removing metmyoglobin are prevented from effecting this repair, or alternatively the rate of metmyoglobin formation exceeds their capacity, so that there is a net accumulation of metmyoglobin as the meat ages.
This has important consequences for the meat packing industry, as brown meat is less aesthetically appealing, and in order to be sold, it is usually downgraded and minced, at a reduced price, resulting in a substantial economic loss.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Metmyoglobin". A list of authors is available in Wikipedia.