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Antioxidant Enzyme Activity, Iron Content and Lipid Oxidation of Raw and Cooked Meat of Korean Native Chickens and Other Poultry
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 Title & Authors
Antioxidant Enzyme Activity, Iron Content and Lipid Oxidation of Raw and Cooked Meat of Korean Native Chickens and Other Poultry
Muhlisin, Muhlisin; Utama, Dicky Tri; Lee, Jae Ho; Choi, Ji Hye; Lee, Sung Ki;
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This study was conducted to observe antioxidant enzyme activity, iron content and lipid oxidation of Korean native chickens and other poultry. The breast and thigh meat of three Korean native chicken breeds including Woorimatdak, Hyunin black and Yeonsan ogye, and three commercial poultry breeds including the broiler, White Leghorn and Pekin duck (Anasplatyrhyncos domesticus) were studied. The analyses of the antioxidant enzymes activity, iron content and lipid oxidation were performed in raw and cooked samples. The activity of catalase (CAT) in the thigh meat was higher than that of the breast meat of three Korean native chickens and the broiler, respectively. The activity of glutathione peroxidase (GPx) in the uncooked thigh meat of three Korean native chickens was higher than that of the breasts. The breast meat of Woorimatdak and Pekin duck had higher superoxide dismutase (SOD) activity than the others, while only the thigh meat of Pekin duck had the highest activity. Cooking inactivated CAT and decreased the activity of GPx and SOD. The thigh meat of Woorimatdak, White Leghorn, Yeonsan ogye and Hyunin black contained more total iron than the breast meat of those breeds. The heme-iron lost during cooking ranged from 3.2% to 14.8%. It is noted that the thigh meat had higher thiobarbituric acid reactive substances values than the breast in all chicken breeds. Though Woorimatdak showed higher antioxidant enzyme activity and lower released-iron percentage among Korean native chickens, no differences were found on lipid oxidation. We confirm that the dark meat of poultry exhibited higher antioxidant enzyme activity and contained more iron than the white meat.
Antioxidant Enzyme Activity;Iron Content;Korean Native Chicken;Lipid Oxidation;
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Aebi, H. E. 1984. Catalase in vitro. Methods Enzymol. 105:121-126. crossref(new window)

Ahn, D. U., F. H. Wolf, and J. S. Sim. 1993. Three methods for determining nonheme iron in turkey meat. J. Food Sci. 58:288-291. crossref(new window)

Bekhit, A. E. D. A., D. L. Hopkins, F. T. Fahri, and E. N. Ponnampalam. 2013. Oxidative processes in muscle systems and fresh meat: Sources, markers, and remedies. Compr. Rev. Food Sci. Food Saf. 12:565-597. crossref(new window)

Buettner, G. R. and B. A. Jurkiewicz. 1996. Catalytic metals, ascorbate and free radicals: combinations to avoid. Radiat. Res. 145:532-541. crossref(new window)

Carter, P. 1971. Spectrophotometric determination of serum iron at the submicrogram level with a new reagent (ferrozine). Anal. Biochem. 40:450-458. crossref(new window)

Chan, K. M. and E. A. Decker. 1994. Endogenous skeletal muscle antioxidants. Crit. Rev. Food Sci. Nutr. 34:403-426. crossref(new window)

Chen, W., H. L. Zhu, Y. Shi, M. M. Zhao, H. Wang, and Y. Q. Zeng. 2012. Comparative analysis on antioxidative ability of muscle between laiwu pig and large white. Asian Australas. J. Anim. Sci. 25:1190-1196. crossref(new window)

Clark, E. M., A. W. Mahoney, and C. E. Carpenter. 1997. Heme and total iron in ready-to-eat chicken. J. Agric. Food Chem. 45:124-126. crossref(new window)

Daun, C. and B. Akesson. 2004. Comparison of glutathione peroxidase activity, and of total and soluble selenium content in two muscles from chicken, turkey, duck, ostrich and lamb. Food Chem. 85:295-303. crossref(new window)

DeVore, V. R., G. R. Colnago, L. S. Jensen, and B. E. Greene. 1983. Thiobarbituric acid values and glutathione peroxidase activity inmeat from chickens fed a selenium-supplemented diet. J. Food Sci. 48:300-301. crossref(new window)

Gatellier, P., Y. Mercier, and M. Renerre. 2004. Effect of diet finishing mode (pasture or mixed diet) on antioxidant status of Charolais bovine meat. Meat Sci. 67:385-394. crossref(new window)

Halliwell, B. and J. M. C. Gutteridge. 1990. Role of free radicals and catalytic metal ions in human disease: An overview. Methods Enzymol. 186:1-85. crossref(new window)

Hernandez, P., L. Zomeno, B. Arino, and A. Blasco. 2004. Antioxidant, lipolytic and proteolytic enzyme activities in pork meat from different genotypes. Meat Sci. 66:525-529. crossref(new window)

Hoac, T., C. Daun, U. Trafikowska, J. Zackrisson, and B. Akesson. 2006. Influence of heat treatment on lipid oxidation and glutathione peroxidase activity in chicken and duck meat. Innov. Food Sci. Emerg. Technol. 7:88-93. crossref(new window)

Hornsey, H. C. 1956. The colour of cooked cured pork. I. Estimation of the nitric oxide-haem pigments. J. Sci. Food Agric. 7:534-540. crossref(new window)

Lawrie, R. 1979. Meat Science. 3rd ed. Pergamon press, Oxford, UK.

Lee, S. K., L. Mei, and E. A. Decker. 1996. Lipid oxidation in cooked turkey as affected by added antioxidant enzymes. J. Food Sci. 61:726-728. crossref(new window)

Lombardi-Boccia, G., B. Martinez-Dominguez, and A. Aguzzi. 2002. Optimization of heme iron analysis in raw and cooked red meat. Food Chem. 78:505-510. crossref(new window)

Marklund, S. and G. Marklund. 1974. Involvement of the superoxide anion radical in the autooxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur. J. Biochem. 47:469-474. crossref(new window)

Mei, L., A. D. Crum, and E. A. Decker. 1994. Development of lipid oxidation and inactivation of antioxidant enzymes in cooked pork and beef. J. Food Lipids 1:273-283. crossref(new window)

Mcmillin, K. W. 2008. Where is MAP going? A review and future potential of modified atmosphere packaging for meat. Meat Sci. 80:43-65. crossref(new window)

Min, B. and D. U. Ahn. 2005. Mechanism of lipid peroxidation in meat and meat products-A review. Food Sci. Biotechnol. 14:152-163.

Min, B., K. C. Nam, J. Cordray, and D. U. Ahn. 2008. Endogenous factors affecting oxidative stability of beef loin, pork loin, and chicken breast and thigh meats. J. Food Sci. 73:439-446.

Pradhan, A. A., K. S. Rhee, and P. Hernandez. 2000. Stability of catalase and its potential role in lipid oxidation in meat. Meat Sci. 54:385-390. crossref(new window)

Renerre, M., F. Dumont, and P. Gatellier. 1996. Antioxidative enzyme activities in relation to oxidation of lipid and myoglobin. Meat Sci. 43:111-121.

Schricker, B. R., D. D. Miller, and J. R. Stouffer. 1982. Measurement and content of nonheme and total iron in muscle. J. Food Sci. 47:740-743. crossref(new window)

Sinnhuber, R. O. and T. C. Yu. 1977. The 2-thiobarbituric acid reaction, an objective measure of the oxidative deterioration occurring in fats and oil. J. Japan Oil Chem. Soc. 26:259-267. crossref(new window)

Terevinto, A., A. Ramos, G. Castroman, M. C. Cabrera, and A. Saadoun. 2010. Oxidative status, in vitro iron-induced lipid oxidation and superoxide dismutase, catalase and glutathione peroxidase activities in rhea meat. Meat Sci. 84:706-710. crossref(new window)