Potravinarstvo Slovak Journal of Food Sciences Volume 11 606 No. 1/2017 Potravinarstvo Slovak Journal of Food Sciences vol. 11, 2017, no. 1, p. 606-611 doi: https://dx.doi.org/10.5219/800 Received: 7 April 2017. Accepted: 27 October 2017. Available online: 30 October 2017 at www.potravinarstvo.com © 2017 Potravinarstvo Slovak Journal of Food Sciences, License: CC BY 3.0 ISSN 1337-0960 (online) THE INVESTIGATION OF ALFALFA EFFECT ON THE ACTIVITY OF SUPEROXIDE DISMUTASE IN CHICKEN MEAT in dependence on TIME STORAGE Jana Tkáčová, Mária Angelovičová, Marcela Capcarová, Adriana Kolesárová, Monika Schneidgenová, Adriana Pavelková, Marek Bobko, Juraj Čuboň ABSTRACT 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. Keywords: oxidation, superoxid dismutase, lucerne meal, meat, chicken, time storage INTRODUCTION Oxidation processes are one of the primary mechanisms of quality deterioration in meat and meat products because they lead to the degradation of lipids and proteins (including haem pigments) and they cause the loss of flavour, colour and nutritive value and limit the shelf-life of meat and meat products (Kanner, 1994; Karwowskaet al., 2007). The mechanisms of oxidative degradation can be autoxidation in presence of atmospheric oxygen (Angelovič et al., 2015). Lipid peroxidation is a primary cause of quality deterioration in meat and meat products. Free radical chain reaction is the mechanism of lipid peroxidation and reactive oxygen species (ROS) such as hydroxyl radical and hydroperoxyl radical are the major initiators of the chain reaction. Lipid peroxyl radical and alkoxyl radical formed from the initial reactions are also capable of abstracting a hydrogen atom from lipid molecules to initiate the chain reaction and propagating the chain reaction (Min and Ahn, 2005). Enzymes such as superoxid dismutase, katalase and glutation peroxidase can prevent of meat oxidation because they have influence to oxidation of muscle fiber (Daun and Akesson, 2004; Tkáčová and Angelovičová, 2013). The superoxide dismutases (SODs) are the first and most important line of antioxidant enzyme defense systems against ROS and particularly superoxide anion radicals. At present, three distinct isoforms of SOD have been identified in mammals, and their genomic structure, cDNA, and proteins have been described (Chang et al., 1988; Keller et al., 1991; Crapo et al., 1992; Liou et al., 1993; Zelko et al., 2002). Superoxide dismutases (SODs) are metalloenzymes found widely distributed in prokaryotic and eukaryotic cells (Fridovich, 1995; Johnson and Giulivi, 2005). These SODs are historically designated, in higher eukaryotes, by their primary location as follows: SOD1 (cytoplasmic), SOD2 (mitochondrial) and SOD3 (extracellular) (Marklund, 1984; Johnson and Giulivi, 2005).