Metmyoglobin reductase activity in porcine m. longissimus dorsi muscle

Meat Science

Volumn 51, Issue 2, 1999, Pages 155-161

  Mikkelsen, Anni ^a   Juncher, Dorte ^a   Skibsted, Leif H ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

Metmyoglobin reductase; Porcine metmyoglobin; Pork colour

Indexed keywords

BOVINAE; EQUIDAE; SUIDAE; SUS SCROFA;

EID: 0033478348     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0309-1740(98)00114-4     Document Type: Article

References (23)

1. Andersen H.J., Bertelsen G., Skibsted L.H. Salt effect on acid-catalyzed autoxidation of oxymyoglobin. Acta Chemica Scandinavia. A42:1988;226-236.
2. Andersen H.J., Skibsted L.H. Kinetics and mechanism of thermal oxidation and photooxidation of the colour of nitrosylmyoglobin in aqueous solution. Journal of Agriculture and Food Chemistry. 40:1992;1741-1750.
3. 5 reductase) system components in bovine skeletal muscle. Meat Science. 39:1995;205-213.
4. 5 reductase. Japanese Journal of Zootechnology and Science. 60:1989;46-56.
5. Bertelsen G., Skibsted L.H. Photooxidation of oxymyoglobin. Wavelength dependence of quantum yield in relation to light discoloration in meat. Meat Science. 19:1987;243-251.
6. Brown W.D., Snyder H.E. Nonenzymatic reduction and oxidation of myoglobin and hemoglobin by nicotinamide adenine dinucleotides and flavins. The Journal of Biological Chemistry. 244:1969;6702-6706.
7. Bruun-Jensen L., Sosniecki L., Skibsted L.H. Pressure effects on acid-catalysed autoxidation of oxymyoglobin. Zeitschrift für Lebensmittel Untersuchung und Forschung. A205:1997;407-410.
8. Buffinton G., Mira D., Galaris D., Hochstein P., Cadenas E. Reduction of ferryl- and metmyoglobin to ferrous myoglobin by menadione-glutathione conjugate. Spectrophotometric studies under aerobic and anaerobic conditions. Chemico-Biological Interactions. 66:1988;205-222.
9. Chan W.K.E., Faustman C., Decker E. Oxymyoglobin oxidation as affected by oxidation products of phosphatidylcholine liposomes. Journal of Food Science. 62:1997;709-712.
10. Cheah P.B., Ledward D.A. Inhibition of metmyoglobin formation in fresh beef by pressure treatment. Meat Science. 45:1997;411-418.
11. Echevarne C., Renerre M., Labas R. Metmyoglobin reductase activity in bovine muscles. Meat Science. 27:1990;161-172.
12. Faustman C., Cassens R.G. The biochemical basis for discoloration in fresh meat: A review. Journal of Muscle Foods. 1:1990;217-243.
13. George P., Stratmann C.J. The oxidation of myoglobin to metmyoglobin by oxygen. II The relation between the first order rate constant and the partial pressure of oxygen. Biochemical Journal. 51:1952;418-425.
14. Hagler L., Coppes R.I., Herman R.H. Metmyoglobin reductase. Identification and purification of a reduced nicotinamide adenine dinucleotide-dependent enzyme from bovine heart which reduces metmyoglobin. Journal of Biological Chemistry. 254:1979;6505-6514.
15. Harada K., Tamura M., Yamazaki I. The 2-electron reduction of sperm whale myoglobin by ethanol. Journal of Biochemistry. 100:1986;499-504.
16. Ledward D.A. Post-slaughter influences on the formation of metmyoglobin in beef muscles. Meat Science. 15:1985;149-171.
17. Ledward, D.A., 1992. Colour of raw and cooked meat. In: Ledward, D.A., Johnston, D.E., Knight, M. (Eds.), The Chemistry of Muscle-based Foods. Royal Society of Chemistry, London, pp. 128-144.
18. 5 interactions and the kinetic mechanism of metmyoglobin reductase. Journal of Biological Chemistry. 260:1985;15699-15707.
19. Madhavi, D.L., Carpenter, C.E., 1993. Aging and processing affect color, metmyoglobin reductase and oxygen consumption of beef muscles. Journal of Food Science 58, 939-942, 947.
20. Mikkelsen A., Skibsted L.H. The kinetics of enzymatic reduction of metmyoglobin in relation to oxygen activation in meat products. Zeitschrift für Lebensmittel Untersuchung und Forschung. 194:1992;9-16.
21. Reddy I.M., Carpenter C.E. Determination of metmyoglobin reductase activity in bovine skeletal muscles. Journal of Food Science. 56:1991;1161-1164.
22. Renerre M., Labas R. Biochemical factors influencing metmyoglobin formation in beef muscles. Meat Science. 19:1987;151-165.
23. Romero F.J., Ordoñez I., Arduini A., Cadenas E. The reactivity of thiols and disulfides with different redox states of myoglobin. Redox and addition reactions and formation of thiyl radical intermediates. Journal of Biological Chemistry. 267:1992;1680-1688.