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High temperature reduction of metmyoglobin in aqueous muscle extracts

Osborn, H.M., Brown, H., Adams, J.B. and Ledward, D.A. (2003) High temperature reduction of metmyoglobin in aqueous muscle extracts. Meat Science, 65 (1). pp. 631-637. ISSN 0309-1740

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To link to this article DOI: 10.1016/s0309-1740(02)00258-9

Abstract/Summary

Oxymyoglobin in aqueous extracts of fresh beef longissimus dorsi muscles was initially oxidised to metmyoglobin during heat treatments at temperatures in the range 50-70 degreesC. The metmyoglobin then underwent reduction to a red pigment that was shown spectrally to be identical to oxymyoglobin. The formation of oxymyoglobin involved a heat induced precipitate that when removed from the solution, allowed oxidation to metmyoglobin to occur. However, on re-addition of the precipitate further reduction to oxymyoglobin took place. Dialysis of the muscle extract prior to heating markedly inhibited the reduction but addition of NADH to the dialysate permitted further reduction. The precipitate plus NADH caused oxymyoglobin formation in the presence of metmyoglobin but neither the precipitate nor NADH alone induced this formation. It is concluded that the initial conversion of oxymyoglobin to metmyoglobin on heating fresh beef muscle extracts was reversible and that the reverse reaction depended on the presence of both NADH and a muscle protein. (C) 2003 Elsevier Science Ltd. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences
ID Code:13107
Uncontrolled Keywords:cooked meat colour, reducing enzymes, beef colour, MYOGLOBIN

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