The investigation of alfaalfa effect on the activity of superoxide dismutase in chicken meat in dependence on time storage
Keywords:oxidation, superoxid dismutase, lucerne meal, meat, chicken, time storage
This study was conducted in order to monitor the effect of adding lucerne meal to chicken feed mixtures. The experiment was conducted at the Department Food Hygiene and Safety, Faculty of Biotechnology and Food Science, Slovak University of Agriculture in Nitra. Chickens for meat production - final type Cobb 500 were used in the experiment. Chickens were placed in boxes all together for one group at the beginning of the experiment and from 14 days of age chickens were divided individually into floor enriched cages. Feeding of chickens lasted 38 days. The experiment was carried out without sex segregation. For the production of a feed composition was used alfalfa (Medicago sativa) as lucerne meal, which was added to the feed at a rate of 4%, namely: starter (HYD-01), growth (HYD-02) and final (HYD-03). The control group did not include the addition of lucerne meal. Chickens were fed ad libitum. Chickens were slaughtered after completion of feeding and the meat samples were taken for analysis. The collected samples were stored at -18 °C. Collected samples of meat were analyzed after slaughter chickens at time intervals of 6, 12 and 18 months. In the experiment was monitored the content of supeoxid dismutase in the chicken meat depending on the length of storage time. Superoxide dismutase content was increasing by storage time, while there were some statistically significant differences between groups.
Al-Haweizy, A., Al-Sardary, S. Y. 2007. Effect of Dehydrated Alfalfa and Ageon Egg Weight, Egg mass, Feedintake, and Feed Conversion efficiency HYLINEW-98 Layers. Slovak J. Anim. Sci., vol. 40, no. 1, p. 19-23.
Angelovič, M., Jablonický, J., Tkáč, Z., Angelovič, M. Oxidative Stability of Fatty Acid Alkyl Esters: a review. Potravinarstvo Slovak Journal of Food Sciences, vol. 9, no. 1, p. 417-426. https://doi.org/10.1016/j.fuproc.2009.06.009
Bannister, J. V., Bannister, W. H., Rotilio, G. 1987. Aspects of the structure, function, and applications of superoxide dismutase. CRC Crit. Rev. Biochem., vol. 22, p. 111-180. https://doi.org/10.3109/10409238709083738
Barriére, C., Centeno, D., Lebert, A., Leroy-Sétrin, S., Berdagué, J. L., Talon, R. 2001. Roles of superoxid dismutase and catalase of Staphylococcus xylosus in the inhibition of linoleic acid oxidation. FEMS Microbiology Letters. 201, 181-185. https://doi.org/10.1111/j.1574-6968.2001.tb10754.x
Bobko, M., Haščík, P., Bobková, A., Kňazovická, V., Tóth, T., Angelovičová, M. 2012. Influence of different plant supplements applied in chicken nutrition on quality of their meat. J. Mikrob. Biot. Food Sci. vol. 1, Special issue, p.1020-1031.
Bonnie, B. T., Choo, Y. M. 2000. Valuable minor constituents of commercial red palm olein: carotenoids, vitamin E, ubiquinone and sterols. J. Oil Palm. Res., vol. 12, p. 14-24.
Buckley D. ., Morrissey P. A., Gray J. I. 1995. Influence of dietary vitamin E on the oxidative stability and quality of pig meat. J. Anim. Sci., 73, 3122-3130. https://doi.org/10.2527/1995.73103122x
Castellini, C., Mugnai, C., Dal Bosco, A. 2002. Effect of organic production system on broiler carcass and meat quality. Meat Science, 60, p. 219-225. https://doi.org/10.1016/s0309-1740(01)00124-3
Crapo, J. D., Oury, T., Rabouille, C., Slot, J. W., Chang, L.-Y. 1992. Copper, zinc superoxide dismutase is primarily a cytosolic protein in human cells. Proc. Natl. Acad. Sci. USA. 89, p. 10405-10409. https://doi.org/10.1073/pnas.89.21.10405
Culotta, V. C., Yang, M., O'Halloran, T. V. 2006. Activation of superoxide dismutases: Putting the metal to the pedal. Biochimica et Biophysica Acta, 1763, p. 747-758. https://doi.org/10.1016/j.bbamcr.2006.05.003
Dansk, L. M. 1971. A role for alfalfa in high efficiency broiler rations. Poult. Sci., vol. 50, p. 1569-1574.
Daun, Ch., Åkesson, B. 2004. Comparison of glutathione peroxidase activity, and of total and soluble selenium content in two muscles from chicken, turkey, duck, ostrich and lamb. Food Chemistry, vol. 85, p. 295-303. https://doi.org/10.1016/j.foodchem.2003.07.009
Dong, X. F., Gao, W. W., Su, J. L., Tong, Dr. J. M., Zhang, Q. 2011. Effects of dietary polysavone (Alfalfa extract) and chlortetracycline supplementation on antioxidation and meat quality in broiler chickens. Journal British Poutry Science, vol. 52, issue 3, p. 302-309. https://doi.org/10.1080/00071668.2011.569008
Engidawork, E., Lubec, G. 2001. Protein expression in Down syndrome brain. Amino Acids, 21, p. 331-361. https://doi.org/10.1007/s007260170001
Faustman C., Chan W. K. M., Schaefer D. M., Havens A. 1998. Beef color update: the role for vitamin E. J. Anim. Sci., 76, 1019-1026. https://doi.org/10.2527/1998.7641019x
Flohé, L., Ötting, F. 1984. Superoxide dismutase assays. Methods in Enzymology. Oxygen Radicals in Biological Systems. B. Isolation, purification, characterization, and assay of antioxygenic enzymes. Vol. 105, p. 93-104. https://doi.org/10.1016/s0076-6879(84)05013-8
Francis, G., Kerem, Z., Makkar, H. P. S., Becker, K. 2002. The biological action of saponins in animal systems: a review. Br. J. Nutr., vol. 88, p. 587-605. https://doi.org/10.1079/bjn2002725
Fridovich, I. 1986. Superoxide dismutase. Adv. Enzymol., vol. 58, p. 61-97.
Fridovich, I. 1995. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64, p. 97-112. https://doi.org/10.1146/annurev.biochem.64.1.97
Gibbs, R. A., Rymer, C., Givens, D. I. 2013. Fatty acid composition of cooked chicken meat and chicken meat products as influenced by price range at retail. Food Chemistry, vol. 138, p. 1749-1756. https://doi.org/10.1016/j.foodchem.2012.11.002
Haak, L., Raes, K., Smet, K., Claeys, E., Paelinck, H., De Smet, S. 2006. Effect of dietary antioxidant and fatty acid supply on the oxidative stability of fresh and cooked pork. Meat Sci., vol. 74, p. 476-486. https://doi.org/10.1016/j.meatsci.2006.04.018
Haskins, K., Kench, J., Powers, K., Bradley, B., Pugazhenthi, S., Reusch, J., McDuffie, M. 2004. Role for oxidative stress in the regeneration of islet beta cells? J. Investig. Med., vol. 52, p. 45-49. https://doi.org/10.1097/00042871-200401000-00025
Houben J. H., Gerris C. V. M. 1998. Effect of the dietary supplementation with vitamin E on colour stability of packaged, sliced pasteurized ham. Meat Sci., 50, p. 421-428. https://doi.org/10.1016/s0309-1740(98)00054-0
Hugo, A., Els, S. P., Bothma, C., De Witt, F. H., Van Der Merwe, H. J., Fair, M. D. 2009. Influence of dietary lipid sources on sensory characteristics of broiler meat. Peer-reviewed paper: 10th World Conference on Animal Production South African Journal of Animal Science, vol. 39, p. 11-14.
Chang, L.,Y., Slot, J. W., Geuze, H. J., Crapo, J. D. 1988. Molecular immunocytochemistry of the CuZn superoxide dismutase in rat hepatocytes. J. Cell Biol., vol. 107, p. 2169-2179.
Johnson, F., Giulivi, C. 2005. Review Superoxide dismutases and their impact upon human health. Molecular Aspects of Medicine, vol. , p. 340-352. https://doi.org/10.1016/j.mam.2005.07.006
Jung, K., Henke, W. 1996. Developmental changes of antioxidant enzymes in kidney and liver from rats. Free Radic. Biol. Med., vol. 20, no. 4, p. 613-617. https://doi.org/10.1016/0891-5849(95)02090-x
Kakko, S., Paivansalo, M., Koistinen, P., Kesaniemi, Y. A., Kinnula, V. L., Savolainen, M. J. 2003.
The signal sequence polymorphism of the MnSOD gene is associated with the degree of carotid atherosclerosis. Atherosclerosis, 168, p. 147-152. https://doi.org/10.1016/s0021-9150(03)00091-1
Kanner, J. 1994. Oxidative processes in meat and meat products: Quality implications. Meat Sci., vol. 36, p. 169-189. https://doi.org/10.1016/0309-1740(94)90040-x
Karwowska, M., Dolatowski, Z. J., Grela, E. R. 2007. Effect of dietary supplementation with extracted alfalfa oxidation stability cooked. Pol. J. Food Nutr. Sci., vol. 57, no. 4(B), p. 271-274.
Keller, G.-A., Warner, T. G., Steimer, K. S., Hallewell, R. A. 1991. Cu,Zn superoxide dismutase is a peroxisomal enzyme in human ﬁbroblasts and hepatoma cells. Proc. Natl. Acad. Sci. USA, vol. 88, p. 7381-7385. https://doi.org/10.1073/pnas.88.16.7381
Liou, W., Chang, L. Y., Geuze, H. J., Strous, G. J., Crapo, J. D., Slot, J. W. 1993. Distribution of CuZn superoxide dismutase in rat liver. Free Radic. Biol. Med., vol. 14, p. 201-207. https://doi.org/10.1016/0891-5849(93)90011-i
Lu, L., Ji, C., Luo, X. G., Liu, B., Yu, S. X. 2006. The effect of supplemental manganese in broiler diets on abdominal fat deposition and meat quality. Animal Feed Science and Technology, vol. 12, p. 49-59. https://doi.org/10.1016/j.anifeedsci.2005.12.005
Marklund, S. L. 1984. Properties of extracellular superoxide dismutase from human lung. Biochem. J., vol. 220, no. 1, p. 269-272. https://doi.org/10.1042/bj2200269
McCord, J. M., Fridovich, I. 1969. Superoxide dismutase. An enzymic function forerythrocuprein (hemocuprein). J. Biol. Chem., vol. 244, p. 6049-6055.
Min, B., Ahn, D. U. 2005. Mechanism of Lipid Peroxidation in Meat and Meat Products -A ReviewFood Sci. Biotechnol., vol. 14, no. 1, p. 152-163.
O'Grady M. N., Maher M., Troy D. J., Moloney A. P., Kerry J. P. 2006. An assessment of dietary supplementation with tea catechins and rosemary extract on the quality of fresh beef. Meat Sci., 73, p. 132-143. https://doi.org/10.1016/j.meatsci.2005.11.008
RANDOX Laboratories Ltd. , Ransod Superoxid dismutase Manual RX Monza.
Rao, A. V., Gurfinkel, D. M. 2000. The bioactivity of saponins: Triterpenoid and steroidal glycosides. Drug Metabol. Drug Interact., vol. 17, p. 211-235. https://doi.org/10.1515/dmdi.2000.17.1-4.211
Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A. Donaldson, D., Goto, J., O'Regan, J. P., Deng, H. X. et al. 1993. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature, 362, p. 59-62. https://doi.org/10.1038/362059a0
Sen, S., Makkar, H. P. S., Becker, K. 1998. Alfalfa saponins and their implications in animal nutrition. J. Agric. Food Chem., vol. 46, p. 131-140. https://doi.org/10.1021/jf970389i
Steinman, H. M. 1982. Copper-zinc superoxide dismutase from caulobacter crescentus cb15 a novel bacteriocuprein form of the enzyme. J. Biol. Chem., vol. 257, p. 10283-10293.
Stochmal, A., Simonet, A. M., Macias, F. A., Oliveira, M. A., Abreu, J. M., Nash, R., Oleszek, W. 2001. Acylated apigenin glycosides from alfalfa (Medicago sativa L.) var. Artal. Phytochemistry, vol. 57, p. 1223-1226. https://doi.org/10.1016/s0031-9422(01)00204-7
Suksombat, W., Buakeeree, K. 2006. Utilization of hedge lucerne meal (Demathus virgatus) as protein supplement in layers diets. Suranaree J. Sci. Technol., vol. 13, no. 2, p. 182-187.
Tkáčová, J., Angelovičová, M. 2013. Antioxidačná aktivita lucernovej múčky a kvalita kuracieho mäsa (Antioxidant activity of lucerne meal and quality of chicken meat.). Nitra : SPU in Nitra, 99 p. ISBN 978-80-552-1116-9.
Tkáčová, J., Angelovičová, M., Haščík, P., Bobko, M. 2015. Oxidative stability of chicken meat during storage influenced by the feeding of alfalfa meal. Potravinarstvo, vol. 9, no. 1, p. 106-111 https://doi.org/10.5219/444
Wenk C. 2003. Herbs and botanicals as feed additives in monogastric animals. Asian-Australasian J. Anim. Sci., 16, p. 282-289. https://doi.org/10.5713/ajas.2003.282
Whitehead, C. C., Mcnab, J. M., Griffin, H. D. 1981. The effects of low dietary concentrations of saponin on liver lipid accumulation and performance in laying hens. Poult. Sci., vol. 22, p. 281-288. https://doi.org/10.1080/00071688108447887
Zelko, I. N., Mariani, T. J., Folz, R.J. 2002. Superoxide dismutase multigene family: A comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. Free Radical Biology and Medicine, vol. 33, no. 3, p. 337-349. https://doi.org/10.1016/s0891-5849(02)00905-x
Zhou, J. Y. Prognon, P. 2006. Raw material enzymatic activity determination: A specific case for validation and comparison of analytical methods - The example of superoxide dismutase (SOD). J. Pharm. Biomed. Anal., vol. 40, p. 1143-1148. https://doi.org/10.1016/j.jpba.2005.09.022
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