Baibai T, Oukhattar L, Moutaouakkil A, Soukri A. 2007. Purification and characterization of glyceraldehyde-3-phosphate dehydrogenase from european pilchard sardina pilchardus. Acta Biochimica et Biophysica Sinica, 39, 947–954. Bao Y, Puolanne E, Ertbjerg P. 2016. Effect of oxygen concentration in modified atmosphere packaging on color and texture of beef patties cooked to different temperatures. Meat Science, 121, 189–195. Barron J T, Gu L, Parrillo J E. 1998. Malate-aspartate shuttle, cytoplasmic nadh redox potential, and energetics in vascular smooth muscle. Journal of Molecular & Cellular Cardiology, 30, 1571–1579.Calnan H, Jacob R H, Pethick D W, Gardner G E. 2016. Production factors influence fresh lamb longissimus colour more than muscle traits such as myoglobin concentration and pH. Meat Science, 119, 41–50. Canto A C, Costa-Lima B R, Suman S P, Monteiro M L, Viana F M, Salim A P, Nair M N, Silva T J, Conte-Junior C A. 2016. Color attributes and oxidative stability of longissimus lumborum and psoas major muscles from Nellore bulls. Meat Science, 121, 19–26. Canto A C, Suman S P, Nair M N, Li S, Rentfrow G, Beach C M, Silva T J, Wheeler T L, Shackelford S D, Grayson A, McKeith R O, King D A. 2015. Differential abundance of sarcoplasmic proteome explains animal effect on beef Longissimus lumborum color stability. Meat Science, 102, 90–98. Gao X G, Xie L, Wang Z Y, Li X M, Luo H L, Ma C W, Dai R T. 2013. Effect of postmortem time on the metmyoglobin reductase activity, oxygen consumption, and colour stability of different lamb muscles. European Food Research and Technology, 236, 579–587. Hunt M C, King A. 2012. AMSA Meat Color Measurement Guidelines. American Meat Science Association. Champaign, Illinois, USA 61820. pp. 1–135. Joseph P, Suman S P, Rentfrow G, Li S, Beach C M. 2012. Proteomics of muscle-specific beef color stability. Journal of Agricultural & Food Chemistry, 60, 3196–3203. Kim Y H. 2008. Lactate dehydrogenase regulation of the metmyoglobin reducing system to improve color stability of bovine muscles through lactate enhancement. Dissertation Abstracts International, 69, 1–115.Kim Y H, Hunt M C, Mancini R A, Seyfert M, Loughin T M, Kropf D H, Smith J S. 2006. Mechanism for lactate-color stabilization in injection-enhanced beef. Journal of Agricultural & Food Chemistry, 54, 7856–7862. Kim Y H, Keeton J T, Smith S B, Berghman L R, Savell J W. 2009a. Role of lactate dehydrogenase in metmyoglobin reduction and color stability of different bovine muscles. Meat Science, 83, 376–382. Kim Y H, Keeton J T, Yang H S, Smith S B, Sawyer J E, Savell J W. 2009b. Color stability and biochemical characteristics of bovine muscles when enhanced with L- or D-potassium lactate in high-oxygen modified atmospheres. Meat Science, 82, 234–240. King D A, Shackelford S D, Kuehn L A, Kemp C M, Rodriguez A B, Thallman R M, Wheeler T L. 2010. Contribution of genetic influences to animal-to-animal variation in myoglobin content and beef lean color stability. Journal of Animal Science, 88, 1160–1167. King D A, Shackelford S D, Rodriguez A B, Wheeler T L. 2011. Effect of time of measurement on the relationship between metmyoglobin reducing activity and oxygen consumption to instrumental measures of beef longissimus color stability. Meat Science, 87, 26–32. Klingenberg M. 1974. Nicotinamide-adenine dinucleotides (NAD, NADP, NADH, NADPH) spectrophotometric and fluorimetric methods. In: Methods of Enzymatic Analysis. 2nd ed. Academic Press, New York and London. pp. 2045–2072.Ledward D A. 1985. Post-slaughter influences on the formation of metyyoglobin in beef muscles. Meat Science, 15, 149–171. Li W, Sauve A A. 2015. NAD(+) content and its role in mitochondria. Methods in Molecular Biology, 1241, 39–48. Luciano G, Monahan F J, Vasta V, Pennisi P, Bella M, Priolo A. 2009. Lipid and colour stability of meat from lambs fed fresh herbage or concentrate. Meat Science, 82, 193–199. Matarneh S K, England E M, Scheffler T L, Oliver E M, Gerrard D E. 2015. Net lactate accumulation and low buffering capacity explain low ultimate pH in the longissimus lumborum of AMPKγ3R200Q mutant pigs. Meat Science, 110, 189–195. McCormick D B, Wright L D. 1971. Nicotinic acid: Analogs and coenzymes. In: Colowick S P, Kaplan N O, eds., Methods in Enzymology. vol. 18. Academic Press, New York and London. pp. 26–27.McKenna D R, Mies P D, Baird B E, Pfeiffer K D, Ellebracht J W, Savell J W. 2005. Biochemical and physical factors affecting discoloration characteristics of 19 bovine muscles. Meat Science, 70, 665–682. Neethling N E, Suman S P, Sigge G O, Hoffman L C. 2016. Muscle-specific colour stability of blesbok (Damaliscus pygargus phillipsi) meat. Meat Science, 119, 69–79. Ramanathan R, Mancini R A, Dady G A. 2011. Effects of pyruvate, succinate, and lactate enhancement on beef longissimus raw color. Meat Science, 88, 424–428. Ramanathan R, Mancini R A, Joseph P, Yin S, Tatiyaborworntham N, Petersson K H, Sun Q, Konda M R. 2011. Effects of lactate on ground lamb color stability and mitochondria-mediated metmyoglobin reduction. Food Chemistry, 126, 166–171. Richards M P. 2013. Redox reactions of myoglobin. Antioxid Redox Signal, 18, 2342–2351. Saleh B, Watts B M. 1968. Substrates and intermediates in the enzymatic reduction of metmyoglobin in ground beef. Journal of Food Science, 33, 353–358. Suman S P, Joseph P. 2013. Myoglobin chemistry and meat color. Annual Review of Food Science and Technology, 4, 79–99. Yin M C, Faustman C. 1993. Influence of temperature, pH, and phospholipid composition upon the stability of myoglobin and phospholipid a liposome model. Journal of Agricultural & Food Chemistry, 41, 853–857. |