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| Comparsion of the Effects of Succinate and NADH on Postmortem Metmyoglobin Redcutase Activity and Beef Colour Stability |
| GAO Xiao-guang, WANG Zhen-yu, TANG Meng-tian, MA Chang-wei , DAI Rui-tong |
1、College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, P.R.China
2、College of Biological Science and Engineering, Hebei University of Science and Technology, Shijiazhuang 050000, P.R.China
3、Institute of Agro-Products Processing Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products
Processing, Ministry of Agriculture, Beijing 100193, P.R.China |
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摘要 In two experiments, the effects of succinate and NADH (reduced nicotinamide adenine dinucleotide) on metmyoglobin reductase activity and electron transport chain-linked metmyoglobin reduction were investigated and compared. In experiment 1, metmyoglobin (MetMb), substrate and inhibitors were incubated with mitochondria. Comparsion of the effects of succinate and NADH on MetMb reduction was investigated. The MetMb percentage in sample treated with 8 mol L-1 succinate decreased by about 69% after 3 h incubation, and the effect was inhibited by the addition of 10 mol L-1 electron transfer chain complex II inhibitor malonic acid; the MetMb percentage in samples treated with 2 mol L-1 NADH decreased by 56% and the effect was inhibited by the addition of 0.02 mol L-1 electron transport chain complex I inhibitor rotenone. These results indicated that electron transport chain played an important role in MetMb reduction. Both complex II and complex I take part in the MetMb reduction in mitochondria through different pathways. NADH-MetMb reduction system was less stable than succinate- MetMb system. In experiment 2, the beef longissimus dorsi muscle was blended with different concentrations of succinate or NADH. Enhancing patties with higher concentration of succinate or NADH improved colour stability in vacuum packaged samples (P<0.05). These results verified that mitochondria electron transport chain is related to the MetMb reduction in meat system.
Abstract In two experiments, the effects of succinate and NADH (reduced nicotinamide adenine dinucleotide) on metmyoglobin reductase activity and electron transport chain-linked metmyoglobin reduction were investigated and compared. In experiment 1, metmyoglobin (MetMb), substrate and inhibitors were incubated with mitochondria. Comparsion of the effects of succinate and NADH on MetMb reduction was investigated. The MetMb percentage in sample treated with 8 mol L-1 succinate decreased by about 69% after 3 h incubation, and the effect was inhibited by the addition of 10 mol L-1 electron transfer chain complex II inhibitor malonic acid; the MetMb percentage in samples treated with 2 mol L-1 NADH decreased by 56% and the effect was inhibited by the addition of 0.02 mol L-1 electron transport chain complex I inhibitor rotenone. These results indicated that electron transport chain played an important role in MetMb reduction. Both complex II and complex I take part in the MetMb reduction in mitochondria through different pathways. NADH-MetMb reduction system was less stable than succinate- MetMb system. In experiment 2, the beef longissimus dorsi muscle was blended with different concentrations of succinate or NADH. Enhancing patties with higher concentration of succinate or NADH improved colour stability in vacuum packaged samples (P<0.05). These results verified that mitochondria electron transport chain is related to the MetMb reduction in meat system.
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Received: 22 February 2013
Accepted:
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| Fund: the financial support by the National Natural Science Foundation of China (31071624). |
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Corresponding Authors:
DAI Rui-tong, Tel: +86-10-62737644, Mobile: 15376776069, Fax: +86-10-62839300, E-mail: dairuitong@hotmail.com
E-mail: dairuitong@hotmail.com
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| About author: GAO Xiao-guang, E-mail: gaoxiaoguang999@126.com |
Cite this article:
GAO Xiao-guang, WANG Zhen-yu, TANG Meng-tian, MA Chang-wei , DAI Rui-tong.
2014.
Comparsion of the Effects of Succinate and NADH on Postmortem Metmyoglobin Redcutase Activity and Beef Colour Stability. Journal of Integrative Agriculture, 13(8): 1817-1826.
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| Arihara K, Cassens R G, Greaser M L, Luchansky J B,Mozdziak P E. 1995. Localization of metmyoglobinreducing enzyme (NADH-cytochrome b5 reductase) system components in bovine skeletal muscle. Meat Science, 39, 205-213Bekhit A E, Faustman C. 2005. Metmyoglobin reducingactivity: a review. Meat Science, 71, 407-439Cimen H, Han M J, Yang Y, Tong Q, Koc H, Koc E C. 2010.Regulation of succinate dehydrogenase activity by SIRT3in mammalian mitochondria. Biochemistry, 49, 304-311Echevarne C, Renerre M, Labas R. 1990. Metmyoglobinreductase activity in bovine muscles. Meat Science, 27,161-172Faustman C, Cassens R G. 1990. The biochemical basis formeat discoloration in fresh meat: a review. Journal ofMuscle Foods, 1, 217-243Hagler L, Coppes Jr. R I, Herman R H. 1979. Metmyoglobinreductase. Identification and purification of a reducednicotinamide adenine dinucleotide-dependent enzyme frombovine heart which reduces metmyoglobin. The Journalof Biological Chemistry, 254, 6505-6514Kim Y H, Hunt M C, Mancini R A, Seyfert M, Loughin TM, Kropf D H, Smith J S. 2006. Mechanism for lactate-color stabilization in injection-enhanced beef. Journal ofAgricultural and Food Chemistry, 54, 7856-7862 Koizumi C, Brown W D. 1972. A peroxidative mechanism for the nonenzymatic reduction of metmyoglobin. Biochimica et Biophysica Acta, 264, 17-24 Lind C, Cadenas E, Hochstein P, Ernster L. 1990. DT-diaphorase: purification, properties, and function. Methods in Enzymology, 186, 287-301 Linvingston D J, Mclachlan S J, Lamar G N, Brown W D. 1985. Myoglobin: cytochrome b5 interactions and the kinetic mechanism of metmyoglobin reductase. The Journal of Biological Chemistry, 260, 15699-15707 Mclaren K. 1987. Colour space, colour scales and colour difference. In: McDonald R, ed., Colour Physics for Industry. 2nd. Dyers Company Publications Trust, Bradford. pp. 97-115 Mikkelsen A, Juncher D, Skibsted L H. 1999. Metmyoglobin reductase activity in porcine m. longissimus dorsi muscle. Meat Science, 51, 155-161 Mikkelsen A, Skibsted L H. 1992. Kinetics of enzymatic reduction of metmyoglobin in relation to oxygen activation in meat products. Zeitschrift für Lebensmittel- Untersuchung und -Forschung (A), 194, 9-16 de Paula Paseto Fernandes R, de Alvarenga Freire M T, Da Costa Carrer C, Trindade M A. 2013. Evaluation of physicochemical, microbiological and sensory stability of frozen stored vacuum-packed lamb meat. Journal of Integrative Agriculture, 12, 1946-1952 Pighin D G, Cunzolo S A, Zimerman M, Pazos A A, Domingo E, Pordomingo A J, Grigioni G. 2013. Impact of adrenaline or cortisol injection on meat quality development of Merino hoggets. Journal of Integrative Agriculture, 12, 1931-1936 Reddy L M, Carpenter C H. 1991. Determination of metmyoglobin reductase activity in bovine skeletal muscles. Journal of Food Science, 56, 1161-1164 Seydim A C, Guzel-Seydim Z B, Acton J C, Dawson P L. 2006. Effects of rosemary extract and sodium lactate on quality of vacuum-packaged ground ostrich meat. Journal of Food Science, 71, S71-S76. Sañudo C, Muela E, Campo M D M. 2013. Key factors involved in lamb quality from farm to fork in Europe. Journal of Integrative Agriculture, 12, 1919-1930 Smith A L. 1967. Preparation, properties, and conditions for assay of mitochondria: Slaughterhouse material, small-scale. Methods in Enzymology, 10, 81-86 Tang J, Faustman C, Hoagland T A. 2004. Krzywicki revisited: Equations for spectrophotometric determination of myoglobin redox forms in aqueous meat extracts. Journal of Food Science, 69, C717-C720. Tang J, Faustman C, Hoagland T A, Mancini R A, Seyfert M, Hunt M C. 2005a. Postmortem oxygen consumption by mitochondria and its effects on myoglobin form and stability. Journal of Agricultural and Food Chemistry, 53, 1223-1230 Tang J, Faustman C, Mancini R A, Seyfert M, Hunt M C. 2005b. Mitochondrial reduction of metmyoglobin: Dependence on the electron transport chain. Journal of Agricultural and Food Chemistry, 53, 5449-5455 Tretter L, Szabados G, Andó A, Horváth I. 1987. Effect of succinate on mitochondrial lipid peroxidation. 2. The protective effect of succinate against functional and structural changes induced by lipid peroxidation. Journal of Bioenergetics and Biomembranes, 19, 31-34 Watts B M, Kendrick J, Zipser M W, Hutchins B, Saleh B. 1966. Enzymatic reducing pathways in meat. Journal of Food Science, 31, 855-862 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 and Food Chemistry, 41, 853-857 Zhu J, Liu F, Li X, Dai R. 2009. Effect of succinate sodium on the metmyoglobin reduction and color stability of beef patties. Journal of Agricultural and Food Chemistry, 57, 5976-5981 |
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