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2014 | 13 | 2 |
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Role of peroxidation and heme catalysis in coloration of raw meat

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It is known, that lipid peroxidation is one of the main factors limiting the quality and acceptability of meat and other animal tissues. The current data conceming connection of heme and peroxidation were summarized and analysed here. The muscle food compounds that are most influenced by oxidative processes include unsaturated fatty acids of lipids, amino acids of proteins and heme groups of pigments. Heme proteins and particularly myoglobin are abundant in muscle tissues. Meat colour is primarily influenced by the concentration and Chemical State of heme pigments, myoglobin and hemoglobin. Oxygenated myoglobin oxidized to the brown metmyoglobin form and its accumulation is highly correlated with progress of lipid peroxidation. Heme proteins such as hemoglobin or myoglobin accelerate the decomposition of hydroperoxides to free radicals. Metmyoglobin possesses «pseudoperoxidase» activity and catalyzes the oxidation of various compounds following the reaction with hydrogen peroxide. The reaction between hydrogen peroxide and metmyoglobin results in the formation of two active hypervalent myoglobin species, perferrylmyoglobin (*MbFeIV=O) and ferrylmyoglobin (MbFeIV=O), which participate in lipid oxidation catalysis. Both MbFeIV=O and *MbFelV=O are deactivated in the presence of reducing agents, whose nature determines the overall effect of the pseudoperoxidase cycle. Hypothesis can be put forward that loss of cellular antioxidants might precede the rise of peroxidase-like activity, thus being a sign of incipient discoloration of meats and muscle components of foods.
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  • Institute of Refrigeration and Biotechnologies, St. Petersburg National Research University of Information Technologies, Mechanics and Optics, St. Petersburg, Russia
  • Moscow Veterinary Clinic, Moscow, Russia
  • Bilska A., 2011. Packaging systems for animal origin food. Logforum 7, 1,4.
  • Dmitriev L.F., 1998. Cytochrome b5 and tocopherol provide functions of lipid-radical cycles and energy conversion in membranes. Biochemistry 63 (10), 1447-1450 [in Russian].
  • Carlsen C.U., Skovgaard I.M., Skibsted L.H., 2003. Pseu- doperoxidase activity of myoglobin: kinetics and mechanism of the peroxidase cycle of myoglobin with H202 and 2,2-azino-bis(3-ethylbenzthiazoline-6-sulfonate) as substrates. 2003. J. Agric. Food Chem. 51. 5815-5823.
  • Chan W.K.M., Faustman C., Yin M., Decker E.A., 1997. Lipid oxidation induced by oxymyog!obin and metmyoglobin with involvement of H202 and superoxide anion. MeatSci. 46, 181-190.
  • Dahl T.A., Midden W.E., Hartman P.R., 1988. Same prevalent biomolecules as defences against singlet oxygen. J. Photochem. Photobiol. 43, 357-362.
  • Dobrucka R., 2013. Future of active and intelligent packaging industry. Logforum 9 (2), 103-110.
  • Gardner H.W., 1989. Oxygen radical chemistry of polyunsaturated fatty acid. Free Radie. Biol. Med. 7, 65-86.
  • Gębicki J.M., 1997. Protein hydroperoxides as new reactive oxygen species. Redox Rep. 3, 99-110.
  • Han D., McMillin K.W., Godber J.S., 1994. Hemoglobin, myoglobin, and total pigments in beef and chicken muscles: chromatographic determination. Food Sci. 59, 1279-1282.
  • Kanner J., Salan M.A., Harel S., Shegalovich I., 1991. Lipid peroxidation of muscle food: The role of cytozolic fraction. J. Agric. Food Chem. 39, 242-246.
  • Karami M., Alimon A.R., Sazili A.Q., Goh Y.M. 2010. Meat quality and lipid oxidation of infraspinatus muscle and blood plasma of goats under dietary supplementation of herbal antioxidants. J. Anim. Vet. Adv. 9 (24), 3039-3047.
  • Koppenol W.H., 1994. Chemistry of iron and copper in radical reactions. In: Free radical damage and its control. Ed. C.A. Rise-Evans, R.H. Burdon. Elsevier Amsterdam, 3-24.
  • Luciano G., Monahan F.J., Vasta V., Pennisi P., Bella M., Priolo A., 2009. Lipid and color stability of meat from lambs fed ffesh herbage or concentrate. Meat Sci. 82 (2), 193-199.
  • Luo S.W., Hultin H.O., 1986. An enzymic-catalyzed lipid oxidation system in troutmuscle mitochondria. 46th Annual Meeting of the Institute of Food Technologists. Dallas, Texas, 15-18 June, 1986.
  • McMillin K.W., 2010. Meat production and quality. In: Goat science and production. Ed. S. Solaiman. Wiley-Blackwell Publ., 255-273.
  • Metelitza D.I., Karasyova E.I., 2007. Initiation and inhibition of free-radical processes in biochemical peroxidase Systems: A review. Appl. Biochem. Microbiol. 43 (5), 537-564 [in Russian],
  • Morrisey P.A., Sheehy P.J.A., Galvin K., Kerry J.P., 1998. Lipid stability in meat and meat products. Meat Sci. 49, 73-86.
  • Niki E., Noguchi N., GotohN., 1992. Dynamics of lipid peroxidation and its inhibition by antioxidants. J. Biochem. Soc. Trans. 21, 313-317.
  • Oertling W.A., Hoogland H., Babcock G.T., Wever R., 1990. Identification and properties of an oxoferryl structure in myeloperoxidase compound II. J. Biochem. 29 (15), 5395-5400.
  • Rhee K.S., Dutson T.R., Savell J.W., 1985. Enzymie lipid peroxidation in beef muscle microsomes as affected electrical stimulation and postmortem muscle excision time. J. Food. Biochem. 9, 27-36.
  • Shleikin A.G., Medvedev Y.V., ShataIov I.S., 2012. Effect of ascorbic acid on the peroxidase activity of muscle tissue. J. Proc. Appar. Pisch. Proizvod. 2, [online], http:// [in Russian],
  • Tiulina O.V., Bychkova O.N., Prokopieva V.D., Boldyrev A.A., 2002. Histidincontaining dipeptides and blood cells. Probl. Gemat. 4, 53-63 [in Russian],
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