Abstract
Protein oxidation is an important chemical process that occurs widely in biological systems. Recent advances in protein research have led to the recognition that muscle proteins, similar to nucleic acids and lipids, can be modified by oxygen free radicals. Such modifications are implicated in the pathogenesis of a number of diseases and certain physiological processes, including aging, ischemia-reperfusion injury, and protein turnover (Stadtman, 1993; Carney and Carney, 1994). Many cellular enzymes, such as alkaline neutral protease involved in protein metabolism, and a number of membrane transport proteins, are susceptible to active oxygen species, and can be readily inactivated due to oxidative damages. Oxidative modification of proteins can occur as a result of attack by free radicals generated via lipid peroxidation, metal ion-catalyzed oxidative reactions, and enzymatic processes (Halliwell and Gutteridge, 1986; Stadtman and Oliver, 1991; Signorini et al., 1995). Free radical-induced physicochemical changes in proteins include protein polymerization (via condensation of protein free radicals), insolubilization, peptide chain scission, and formation of lipid-protein complex (Schaich, 1980; Hanan and Shaklai, 1995).
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References
Bhoite-Solomon, V., Kessler-Icekson, G., and Shaklai, N., 1992, Peroxidative crosslinking of myosins, Biochem. Int. 26:181–189.
Carney, J.M., and Carney, A.M., 1994, Role of protein oxidation in aging and in age-associated neurodegenerative diseases, Life Sci. 55:2097–2103.
Caughley, W.S., and Watkins, J.A., 1985, Oxy radical and peroxide formation by hemoglobin and myoglobin, in: CRC Handbook of Methods for Oxygen Radical Research, R.A. Greenwald, ed., CRC Press, Boca Raton, FL.
Decker, E.A., Xiong, Y.L., Calvert, J.T., Crum, A.D., and Blanchard, S.P., 1993, Chemical, physical and functional properties of oxidized turkey white muscle myofibrillar proteins, J. Agric. Food Chem. 41:186–189.
Doba, T., Burton, G.W., and Ingold, K.U, 1985, Antioxidant and co-antioxidant activity of vitamin C. The effect of vitamin C, either alone or in the presence of vitamin E or a water-soluble vitamin E analogue, upon the peroxidation of aqueous multilamellar phospholipid liposomes, Biochim. Biophys. Acta 835:298–303.
Elkassabany, Y., and Hoseney, R.C., 1980, Ascorbic acid as an oxidant in wheat flour dough. II. Rheological effects, Cereal Chem. 57:88–91.
Greene, B.E., 1969, Lipid oxidation and pigment changes in raw beef, J. Food Sci. 4:110–113.
Halliwell, B., and Gutteridge, J.M.C., 1986, Oxygen free radicals and iron in relation to biology and medicine: Some problems and concepts, Arch. Biochem. Biophys. 246:501–514.
Hanan, T., and Shaklai, N., 1995, The role of H2O2-generated myoglobin radical in crosslinking of myosin, Free Radic. Res. 22:215–217.
Jarenback, L., and Liljemark, A., 1975, Ultrastructural changes during frozen storage of cod. III. Effects of linoleic acid and linoleic acid hydroperoxides on myofibrillar proteins, J. Food Technol. 10:437–452.
Kelleher, S.D., Hultin, H.O., and Wilhelm, K.A., 1994, Stability of mackerel surimi prepared under lipid-stabilizing processing conditions, J. Food Sci. 59:269–271.
Lee, H.G., Lee, C.M., Chung, K.H., and Lavery, S.A., 1992, Sodium ascorbate affects surimi gel-forming properties, J. Food Sci. 57:1343–1347.
Levine, R.L., Garland, D., Oliver, C.N., Amici, A., Climent, L, Lenz, A.-G., Ahn, B.-W., Shalitel, S., and Stadtman, E.R., 1990, Determination of carbonyl content in oxidatively modified proteins, Meth. Enzymol. 186:464–478.
Liu, G., and Xiong, Y.L., 1996a, Storage stability of antioxidant-washed myofibrils from chicken white and red muscle, J. Food Sci. 61:(in press).
Liu, G., and Xiong, Y.L., 1996b, Contribution of lipid and protein oxidation to rheological differences between chicken white and red myofibrillar proteins, J. Agric. Food Chem. 44:(in press).
McDonald, R.E., and Hultin, H.O., 1987, Some characteristics of the enzymic lipid peroxidation system in the microsomal fraction of flounder skeletal muscle, J. Food Sci. 52:15–21,27.
Nishimura, K., Ohishi, N., Tanaka, Y., and Sasakura, C, 1992, Participation of radicals in polymerization by ascorbic acid of crude actomyosin from frozen surimi of Alaska pollack during a 40°C incubation, Biosci. Biotech. Biochem. 56:24–28.
Schaich, K.M., 1980, Free radical initiation in proteins and amino acids by ionizing and ultraviolet radiations and lipid oxidation — part III: free radical transfer from oxidizing lipids, CRC Crit. Rev. Food Sci. Nutr. 13:189–244.
Shahidi, F., Rubin, L.J., and Wood, D.F., 1987, Control of lipid oxidation in cooked meats by combinations of antioxidants and chelators, Food Chem. 23:151–157.
Signorini, C, Ferrali, M., Ciccoli, L., Sugherini, L., Magnani, A., and Comporti, M., 1995, Iron release, membrane protein oxidation and erythrocyte ageing, FEBS Lett. 362:165–170.
Smith, D.M., 1987, Functional and biochemical changes in deboned turkey due to frozen storage and lipid oxidation, J. Food Sci. 52:22–27.
Snyder, S.L., and Sobocinski, P.Z., 1975, An improved 2,4,6-trinitrobenzenesulfonic acid method for the determination of amines, Anal. Biochem. 64:284–288.
Srinivasan, S., and Hultin Herbert, O., 1995, Hydroxyl radical modification of fish muscle proteins, J. Food Biochem. 18:405–425.
Srinivasan, S., and Xiong, Y.L., 1996, Gelation of beef heart surimi as affected by antioxidants, J. Food Sci. 61:(in press).
Srinivasan, S., Xiong, Y.L., and Decker, E.A., 1996, Inhibition of protein and lipid oxidation in beef heart surimi-like material by antioxidants and combinations of pH, NaCl, and buffer type in the washing media, J. Agric. Food Chem. 44:(in press).
Stadtman, E.R., 1993, Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions, Annu. Rev. Biochem. 62:797–821.
Stadtman, E.R., and Oliver, C.N., 1991, Metal-catalyzed oxidation of proteins, J. Biol. Chem. 266:2005–2008.
Takenaka, Y., Yasuda, H., and Mino, M., 1991, The effect of α-tocopherol as an antioxidant on the oxidation of membrane protein thiols induced by free radicals generated in different sites, Arch. Biochem. Biophys. 285:344–350.
Wan, L., Xiong, Y.L., and Decker, E.A., 1993, Inhibition of oxidation during washing improves the functionality of bovine cardiac myofibrillar protein, J. Agric. Food Chem. 41:2267–2271.
Xiong, Y.L., 1993, A comparison of the rheological characteristics of different fractions of chicken myofibrillar proteins, J. Food Biochem. 16:217–227.
Xiong, Y.L., 1994, Myofibrillar protein from different muscle fiber types: implications of biochemical and functional properties in meat processing, CRC Criu. Rev. Food Sci. Nutr. 34:293–320.
Xiong, Y.L., and Blanchard, S.P., 1994, Myofibrillar protein gelation: viscoelastic changes related to heating procedures, J. Food Sci. 59:734–738.
Xiong, Y.L., Decker, E.A., Robe, G.H., and Moody, W.G., 1993, Gelation of crude myofibrillar protein isolated from beef heart under antioxidative conditions, J. Food Sci. 58:1241–1244.
Yang, T.S., and Froning, G.W., 1992, Effects of pH and mixing time on protein solubility during the washing of mechanically deboned chicken meat, J. Muscle Foods 3:15–23.
Yin, M.C., Faustman, C., Riesen, J.W., and Williams, S.N., 1993, Alpha-tocopherol and ascorbate delay oxymyoglobin and phospholipid oxidation in vitro, J. Food Sci. 58:1273–1276.
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Xiong, Y.L., Srinivasan, S., Liu, G. (1997). Modification of Muscle Protein Functionality by Antioxidants. In: Damodaran, S. (eds) Food Proteins and Lipids. Advances in Experimental Medicine and Biology, vol 415. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1792-8_7
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DOI: https://doi.org/10.1007/978-1-4899-1792-8_7
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