Comparative Analysis on Antioxidative Ability of Muscle between Laiwu Pig and Large White
1
조회
0
다운로드
2
인용
0
참고문헌
키워드
초록
This study was conducted to evaluate effects of storage temperatures (4℃ and 20℃) and pig breeds (Laiwu pig and Large White pig) on the main antioxidative enzymes (superoxide dismutase, catalase, and glutathione peroxidase) activity and lipid oxidation in porcine Longissimus dorsi muscle. Activities of antioxidative enzymes (AOE) decreased slightly during storage, regardless of storage temperatures. Muscle antioxidative enzymes activities stored at 4℃ were higher than that stored at 20℃. Laiwu pig’s enzymes activities were significantly (p<0.01) higher than Large White’s. The level of malondialdehyde is a direct expression of the grade of lipid oxidation in meat. In our study, the malondialdehyde contents increased after 6 days storage. However, malondialdehyde contents of Laiwu pig were significantly (p<0.01) lower than Large White’s. A lower content of malondialdehyde corresponds to a lower oxidation of lipids. These results indicated the muscle antioxidative ability of Laiwu pig was higher than Large White pig. It also implied that antioxidative enzymes were involved in the essentials and deciding mechanisms of meat quality by quenching oxygen free radicals and inhibiting lipid oxidation in muscle.
Abstract
This study was conducted to evaluate effects of storage temperatures (4℃ and 20℃) and pig breeds (Laiwu pig and Large White pig) on the main antioxidative enzymes (superoxide dismutase, catalase, and glutathione peroxidase) activity and lipid oxidation in porcine Longissimus dorsi muscle. Activities of antioxidative enzymes (AOE) decreased slightly during storage, regardless of storage temperatures. Muscle antioxidative enzymes activities stored at 4℃ were higher than that stored at 20℃. Laiwu pig’s enzymes activities were significantly (p<0.01) higher than Large White’s. The level of malondialdehyde is a direct expression of the grade of lipid oxidation in meat. In our study, the malondialdehyde contents increased after 6 days storage. However, malondialdehyde contents of Laiwu pig were significantly (p<0.01) lower than Large White’s. A lower content of malondialdehyde corresponds to a lower oxidation of lipids. These results indicated the muscle antioxidative ability of Laiwu pig was higher than Large White pig. It also implied that antioxidative enzymes were involved in the essentials and deciding mechanisms of meat quality by quenching oxygen free radicals and inhibiting lipid oxidation in muscle.
참고문헌 (24)
- Chan, K. M., "Endogenous skeletal muscle antioxidants", Crit. Rev. Food Sci. Nutr, 34, pp.403~426 (1994)
- Chen, W., "Effects of phospholipid hydroperoxide glutathione peroxidase mRNA expression on meat quality of M.Longissimus dorsi in pigs", Eur. Food Res. Technol, 232, pp.433~440 (2011)
- Daun, C., "Comparison of glutathione peroxidase activity, and of total and soluble selenium content in two muscles from chicken, turkey, duck, ostrich and lamb", Food Chem, 85, pp.295~303 (2004)
- Decker, E. A., "Minimizing rancidity in muscle foods", Food Technol, 52, pp.54~59 (1998)
- Del Rio, D., "A review of recent studies on malondialdehyde as toxic molecule and biological marker of oxidative stress", Nutr. Metab. Cardiovasc. Dis, 15, pp.316~328 (2005)
- Descalzo, A. M., "Influence of pasture or grain-based diets supplemented with vitamin E on antioxidant", oxidative balance of Argentine beef, 2005, pp.70, 35~44
- Descalzo, A. M., "Antioxidant enzymes activity in Psoas major beef muscle from different production systems", Proceedings of the 46th international congress of meat science and technology, 2, pp.560~561 (2000)
- Descalzo, A. M., "A review of natural antioxidants and their effects on oxidative status, odor and quality of fresh beef produced in Argentina", Meat Sci, 79, pp.423~436 (2008)
- Dobretsov, G. E., "The increase of phospholipid bilayer rigidity after lipid peroxidation", FEBS Lett, 84, pp.125~128 (1977)
- Eriksson, C. E., "Lipid oxidation catalysts and inhibitors in raw materials and processed foods", Food Chem, 9, pp.3~19 (1982)
- Fernández, J., "Thiobarbituric acid test for monitoring lipid oxidation in meat", Food Chem, 59, pp.345~353 (1997)
- Gatellier, P., "Effect of diet finishing mode (pasture or mixed diet) on antioxidant status of Charolais bovine meat", Meat Sci, 67, pp.385~394 (2004)
- Gopalakrishnan, J., "Antioxidant activity of mechanically separated pork extracts", Meat Sci, 52, pp.101~110 (1999)
- Hernández, P., "Antioxidant, lipolytic and proteolytic enzyme activities in pork meat from different genotypes", Meat Sci, 66, pp.525~529 (2004)
- Li, H., "Changes of superoxide dismutase activity and malondialdehyde level in postmortem muscle and their association with meat quality in pigs", Acta Veterinaria et Zootechnica Sinica, 41, pp.257~261 (2010)
- Li, S. J., "Lipid oxidation and myosin denaturation in dark chicken meat", J. Agric. Food Chem, 44, pp.3080~3084 (1996)
- Maraschiello, C., "Glutathione peroxidase activity, TBARS, and α-tocopherol in meat from chickens fed different diets", J. Agric. Food Chem, 47, pp.867~872 (1999)
- Mercier, Y., "Lipid and protein oxidation in vitro, and antioxidant potential in meat from Charolais cows finished on pasture or mixed diet", Meat Sci, 66, pp.467~473 (2004)
- Pradhan, A. A., "Stability of catalase and its potential role in lipid oxidation in meat", Meat Sci, 54, pp.385~390 (2000)
- Renerre, M., "Antioxidant enzyme activities in beef in relation to oxidation of lipid and myoglobin", Meat Sci, 43, pp.111~121 (1996)
- Rowe, L. J., "Oxidative environments decrease tenderization of beef steaks through inactivation of μ-calpain", J. Anim. Sci, 82, pp.3254~3266 (2004)
- Terevinto, A., "Oxidative status, in vitro iron-induced lipid oxidation and superoxide dismutase, catalase and glutathione peroxidase activities in rhea meat", Meat Sci, 84, pp.706~710 (2010)
- van der Wal, P. G., "Causes for variation in pork quality", Meat Sci, 46, pp.319~327 (1997)
- Xia, X., "Physicochemical change and protein oxidation in porcine Longissimus dorsi as influenced by different freeze-thaw cycles", Meat Sci, 83, pp.239~245 (2009)
