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Effects of Ozone-Induced Oxidation on the Physicochemical Properties of Myofibrillar Proteins Recovered from Bighead Carp (Hypophthalmichthys nobilis)

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Abstract

The effect of oxidation with ozone on myofibrillar proteins from bighead carp (Hypophthalmichthys nobilis) and its influence on the textural properties of surimi gels of bighead carp were investigated. Treatment with ozone of an appropriate concentration significantly increased the salt extractable protein (SEP), Ca2+-ATPase activity, total sulfhydryl and active sulfhydryl contents, surface hydrophobicity, and carbonyl content of the myofibrillar proteins. The breaking force and deformation of the surimi gels of bighead carp initially increased and subsequently decreased as the extent of oxidation increased. Based on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis, there were no apparent changes in the protein distribution and no new patterns appeared in electrophoresis processing analysis after the ozone treatment. Differential scanning calorimetry (DSC) found that low concentrations of ozone water rinse had slight effects on thermal stabilities of myofibrillar proteins, which coincided with the above results. The present study indicates that ozone treatment is a prospectively mild oxidation protocol for enhancing the physicochemical properties of fish proteins from bighead carp.

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References

  • Auh, J. H., Lee, H. G., Kim, J. W., Kim, J. C., Yoon, H. S., & Park, K. H. (1999). Highly concentrated branched oligosaccharides as cryoprotectant for surimi. Journal of Food Science, 64(3), 418–422.

    Article  CAS  Google Scholar 

  • Benjakul, S., Visessanguan, W., Ishizaki, S., & Tanaka, M. (2001). Differences in gelation characteristics of natural actomyosin from two species of bigeye snapper, priacanthus tayenus and priacanthus macracanthus. Journal of Food Science, 66(9), 1311–1318.

    Article  CAS  Google Scholar 

  • Benjakul, S., Visessanguan, W., Thongkaew, C., & Tanaka, M. (2003). Comparative study on physicochemical changes of muscle proteins from some tropical fish during frozen storage. Food Research International, 36(8), 787–795.

    Article  CAS  Google Scholar 

  • Blanco-Pascual, N., Fernández-Martín, F., & Montero, M. P. (2013). Effect of different protein extracts from Dosidicus gigas muscle co-products on edible films development. Food Hydrocolloids, 33(1), 118–131.

    Article  CAS  Google Scholar 

  • Campos, C. A., Losada, V., Rodriguez, O., Aubourg, S. P., & Barros-Velazquez, J. (2006). Evaluation of an ozone-slurry ice combined refrigeration system for the storage of farmed turbot (Psetta maxima). Food Chemistry, 97(2), 223–230.

    Article  CAS  Google Scholar 

  • Cataldo, F. (2003). On the action of ozone on proteins. Polymer Degradation and Stability, 82, 105–114.

    Article  CAS  Google Scholar 

  • Charles, H. S. (2008). Differential scanning calorimetry. Methods in Cell Biology, 84, 115–141.

    Article  Google Scholar 

  • Choe, E., & Min, D. B. (2006). Chemistry and reactions of reactive oxygen species in foods. Critical Reviews in Food Science and Nutrition, 46, 1–22.

    Article  CAS  Google Scholar 

  • Ellman, G. L. (1959). Tissue sulfhydryl groups. Archives of Biochemistry and Biophysics, 82, 70–77.

    Article  CAS  Google Scholar 

  • Fagan, J. M., Sleczka, B. G., & Sohar, I. (1999). Quantitation of oxidative damage to tissue proteins. International Journal of Biochemistry and Cell Biology, 31(7), 751–757.

    Article  CAS  Google Scholar 

  • Glaze, W. H. (1986). Reaction products of ozone: a review. Environmental Health Perspectives, 69, 151–157.

    Article  CAS  Google Scholar 

  • Gómez-Estaca, J., Montero, P., & Gómez-Guillén, M. C. (2014). Shrimp (Litopenaeus vannamei) muscle proteins as source to develop edible films. Food Hydrocolloids, 41, 86–94.

    Article  Google Scholar 

  • Goncalves, A. A. (2009). Ozone—an emerging technology for the seafood industry. Brazilian Archives of Biology and Technology, 52(6), 1527–1539.

    Article  CAS  Google Scholar 

  • Gornall, A. G., Bardawill, C. J., & David, M. M. (1949). Determination of serum proteins by means of the biuret reaction. The Journal of Biological Chemistry, 177(2), 751–766.

    CAS  Google Scholar 

  • Jiang, S. T., Ho, M. L., Jiang, S. H., Lo, L., & Chen, H. C. (1998). Color and quality of mackerel surimi as affected by alkaline washing and ozonation. Journal of Food Science, 63(4), 652–655.

    Article  CAS  Google Scholar 

  • Kelly, F. J., & Mudway, I. S. (2003). Protein oxidation at the air lung interface. Amino Acids, 25, 375–396.

    Article  CAS  Google Scholar 

  • Kim, J., Yousef, A., & Dave, S. (1999). Application of ozone for enhancing the microbiological safety and quality of foods: a review. Journal of Food Protection, 62, 1071–1087.

    CAS  Google Scholar 

  • Koetters, J., Prahst, A., Skura, B., Rosenthal, H., Black, E. A., & Rodigues-Lopez, J. (1997). Observations and experiments on extending shelf-life of ‘rockfish’ (Sebastes spp.) products with ozone. Journal of Applied Ichthyology, 13(1), 1–8.

    Article  Google Scholar 

  • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685.

    Article  CAS  Google Scholar 

  • Lametsch, R., Roepstorff, P., Møller, H., & Bendixen, E. (2004). Identification of myofibrillar substrates for μ-calpain. Meat Science, 68(4), 515–521.

    Article  CAS  Google Scholar 

  • Lanier, T. C. (1992). Measurement of surimi composition and functional properties. In T. C. Lanier & C. M. Lee (Eds.), Surimi technology (pp. 123–166). New York: Marcel Dekker, Inc.

    Google Scholar 

  • Lanier, T. C. (2000). Surimi gelation chemistry. In J. W. Park (Ed.), Surimi and surimi seafood (pp. 237–265). New York: Marcel Dekker.

    Google Scholar 

  • Liu, G., & Xiong, Y. L. L. (2000). Oxidatively induced chemical changes and interactions of mixed myosin, beta-lactoglobulin and soy 7S globulin. Journal of the Science of Food and Agriculture, 80(11), 1601–1607.

    Article  CAS  Google Scholar 

  • Liu, G., Xiong, Y. L., & Butterfield, D. A. (2000). Chemical, physical, and gel-forming properties of oxidized myofibrils and whey- and soy-protein isolates. Journal of Food Science, 65(5), 811–818.

    Article  CAS  Google Scholar 

  • Lund, M. N., Heinonen, M., Baron, C. P., & Estevez, M. (2011). Protein oxidation in muscle foods: a review. Molecular Nutrition & Food Research, 55(1), 83–95.

    Article  CAS  Google Scholar 

  • MacDonald, G. A., & Lanier, T. C. (1994). Actomyosin stabilization to freeze-thaw and heat denaturation by lactate salts. Journal of Food Science, 59, 101–105.

    Article  CAS  Google Scholar 

  • Mallevaille, J., & Suffet, I. H. (1987). Identification and treatment of tastes and odors in drinking water (p. 292). Denver: Cooperative research report of the AWWA Research Foundation and Lyonnnaise des Eaux.

    Google Scholar 

  • Martinaud, A., Mercier, Y., Marinova, P., Tassy, C., Gatellier, P., & Renerre, M. (1997). Comparison of oxidative processes on myofibrillar proteins from beef during maturation and by different model oxidation systems. Journal of Agricultural and Food Chemistry, 45(7), 2481–2487.

    Article  CAS  Google Scholar 

  • Mielcke, J., & Ried, A. (2004). Current state of application of ozone and UV for food processing. Paper presented at Proceedings of the Food Protection International Conference 2004. Monte da Caparica, Portugal, 20–22 May 2004.

  • Morioka, T., Motoyama, N., Hoshikawa, H., Murakami, A., Okada, M., & Moniwa, T. (1993). Kinetic analysis on the effects of dissolved inorganic and organic substances in raw water on the ozonation of geosmin and 2-MIB. Ozone Science & Engineering, 15(1), 1–18.

    Article  CAS  Google Scholar 

  • Mudd, J. B., Leavitt, R., Ongun, A., & McManus, T. T. (1969). Reaction of ozone with amino acids and proteins. Atmospheric Environment, 3(6), 669–682.

    Article  CAS  Google Scholar 

  • Persson, P. E. (1980). Sensory properties and analysis of two muddy odor compounds in water and fish. Water Research, 14, 1113–1118.

    Article  CAS  Google Scholar 

  • Privalov, P. L., & Khechinashvili, N. N. (1974). A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. Journal of Molecular Biology, 86(3), 665–684.

    Article  CAS  Google Scholar 

  • Qiu, C., Xia, W., & Jiang, Q. (2014). Pressure-induced changes of silver carp (Hypophthalmichthys molitrix) myofibrillar protein structure. European Food Research and Technology, 238(5), 753–761.

    Article  CAS  Google Scholar 

  • Ramirez, J. A., Martin-Polo, M. O., & Bandman, E. (2000). Fish myosin aggregation as affected by freezing and initial physical state. Journal of Food Science, 65, 556–560.

    Article  CAS  Google Scholar 

  • Sante-Lhoutellier, V., Aubry, L., & Gatellier, P. (2007). Effect of oxidation on in vitro digestibility of skeletal muscle myofibrillar proteins. Journal of Agricultural and Food Chemistry, 55(13), 5343–5348.

    Article  CAS  Google Scholar 

  • Shigeru, H., & Shuryo, N. (1985). Contribution of hydrophobicity, net charge and sulfhydryl groups to thermal properties of ovalbumin. Canadian Institute of Food Science and Technology Journal, 18(4), 290–295.

    Article  Google Scholar 

  • Srinivasan, S., & Hultin, H. O. (1997). Chemical, physical, and functional properties of cod proteins modified by a nonenzymic free-radical-generating system. Journal of Agricultural and Food Chemistry, 45(2), 310–320.

    Article  CAS  Google Scholar 

  • Stadtman, E. R., & Berlett, B. S. (1997). Reactive oxygen-mediated protein oxidation in aging and disease. Chemical Research in Toxicology, 10(5), 485–494.

    Article  CAS  Google Scholar 

  • Stadtman, E. R., & Levine, R. L. (2003). Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino Acids, 25, 207–218.

    Article  CAS  Google Scholar 

  • Sun, W., Cui, C., Zhao, M., Zhao, Q., & Yang, B. (2011). Effects of composition and oxidation of proteins on their solubility, aggregation and proteolytic susceptibility during processing of Cantonese sausage. Food Chemistry, 124(1), 336–341.

    Article  CAS  Google Scholar 

  • Sych, J., Lacroix, C., Adambounou, L. T., & Castaigne, F. (1990). Cryoprotective effects of lacticol, palatinit and polydextrose on cod surimi proteins during frozen storage. Journal of Food Science, 55(2), 356–360.

    Article  CAS  Google Scholar 

  • Tyre, C. L., & Chong, M. L. (1992). Surimi technology. New York: Marcel Dekker.

    Google Scholar 

  • Vaz-Velho, M., Silva, M., Pessoa, J., & Gibbs, P. (2006). Inactivation by ozone of Listeria innocua on salmon-trout during cold-smoke processing. Food Control, 17(8), 609–616.

    Article  CAS  Google Scholar 

  • Watanabe, T., Kitabatake, N., & Doi, E. (1988). Protective effects of nonionic surfactants against denaturation of rabbit skeletal myosin by freezing and thawing. Agricultural and Biological Chemistry, 25, 2517–2523.

    Article  Google Scholar 

  • Wright, D. J., Leach, I. B., & Wilding, P. (1977). Differential scanning calorimetric studies of muscle and its constituent proteins. Journal of the Science of Food and Agriculture, 28(6), 557–564.

    Article  CAS  Google Scholar 

  • Wu, W., Zhang, C., Kong, X., & Hua, Y. (2009). Oxidative modification of soy protein by peroxyl radicals. Food Chemistry, 116(1), 295–301.

    Article  CAS  Google Scholar 

  • Xiong, Y. L. L. (1994). Myofibrillar protein from different muscle-fiber types—implications of biochemical and functional-properties in meat processing. Critical Reviews in Food Science and Nutrition, 34(3), 293–320.

    Article  CAS  Google Scholar 

  • Zaman, Z., Sneyers, L., Vanorshoven, A., Blanckaert, N., & Marien, G. (1995). Elimination of paraprotein interference in determination of plasma inorganic phosphate by ammonium molybdate method. Clinical Chemistry, 41(4), 609–614.

    CAS  Google Scholar 

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Acknowledgments

This study was supported by the national natural science funds (31371791), special funds for scientific research on public causes (201305013), special funds for “Taishan Scholars” construction project, the Program for Changjiang Scholars and Innovative Research Team in University, and the most important open fund projects in Zhejiang province (xkzsc06).

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Correspondence to Yong Xue.

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Zhang, T., Xue, Y., Li, Z. et al. Effects of Ozone-Induced Oxidation on the Physicochemical Properties of Myofibrillar Proteins Recovered from Bighead Carp (Hypophthalmichthys nobilis). Food Bioprocess Technol 8, 181–190 (2015). https://doi.org/10.1007/s11947-014-1396-5

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  • DOI: https://doi.org/10.1007/s11947-014-1396-5

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