Document Detail

High temperature reduction of metmyoglobin in aqueous muscle extracts.
MedLine Citation:
PMID:  22063258     Owner:  NLM     Status:  In-Data-Review    
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 °C. 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.
H M Osborn; H Brown; J B Adams; D A Ledward
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Meat science     Volume:  65     ISSN:  0309-1740     ISO Abbreviation:  Meat Sci.     Publication Date:  2003 Sep 
Date Detail:
Created Date:  2011-11-08     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101160862     Medline TA:  Meat Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  631-7     Citation Subset:  -    
The University of Reading, School of Food Biosciences, PO Box 226, Whiteknights, Reading RG6 6AP, UK.
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