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Effects of Non-meat Protein Binders and Acidification on the Efficiency of Cold-Set Pork Restructuring by High Pressure

  • Hong, Geun-Pyo (Department of Food Science and Biotechnology of Animal Resources, Konkuk University) ;
  • Chun, Ji-Yeon (Department of Food Science and Biotechnology of Animal Resources, Konkuk University) ;
  • Lee, Si-Kyung (Department of Molecular Biotechnology, Konkuk University) ;
  • Choi, Mi-Jung (Department of Molecular Biotechnology, Konkuk University)
  • Received : 2012.03.24
  • Accepted : 2012.05.31
  • Published : 2012.06.30

Abstract

We investigated the effects of non-meat protein binders combined with glucono-${\delta}$-lactone (GdL) on the binding properties regarding restructured pork prepared by high-pressure treatment. Soy protein isolate (SPI), casein (CS), whey protein concentrate (WPC), and egg white (EW) were used as non-meat protein binders and compared with the control (no binder) and with the ${\kappa}$-carrageenan (KC) treatment. The compression and depression rates were 2.3 and 37 MPa/s, respectively, and pressurization was conducted at 200 MPa for 30 min at $4^{\circ}C$. After pressurization, the physical properties (pH, water-holding capacity, color, tensile strength, and microscopic structure) of the sample were evaluated. The combination of pressurization with acidification enabled cold-set meat binding, and the binding strength of restructured pork was enhanced by the addition of non-meat proteins. Among binders, SPI demonstrated the best efficiency in binding meat pieces. Therefore, the present study demonstrated that the combination of acidification and pressurization processes with the utilization of non-meat protein binders has a potential benefit in meat restructuring.

Keywords

References

  1. Aaslyng, M. D. (2002) Quality indicators for raw meat. In: Meat processing: improving quality. Kerry, J., Kerry, J. and Ledward, D. (eds) Limited and Wood head Publishing, CRC Press LLC, FL, pp. 157-174.
  2. AOAC (1990) Official methods of analysis. (15th ed.). Association of Official Analytical Chemists, Washington, DC.
  3. Boonyaratanakornkit, B. B., Park, C. B., and Clark, D. S. (2002) Pressure effects on intra- and intermolecular interactions within proteins. Biochim. Biophys. Acta. 1595, 235-249. https://doi.org/10.1016/S0167-4838(01)00347-8
  4. Bringe, N. A. and Kinsella, J. E. (1990) Acidic coagulation of casein micelles: mechanisms inferred from spectrophotometric studies. J. Dairy Res. 57, 365-375. https://doi.org/10.1017/S0022029900027023
  5. Bryant, C. M. and McClements, D. J. (1998) Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey. Trend. Food Sci. Technol. 9, 143-151. https://doi.org/10.1016/S0924-2244(98)00031-4
  6. Campbell, L., Raikos, V., and Euston, S. R. (2003) Modification of functional properties of egg-white proteins. Nahrung. 47, 369-376. https://doi.org/10.1002/food.200390084
  7. Chin, K. B., Go, M. Y., and Xiong, Y. L. (2009) Konjac flour improved textural and water retention properties of transglutaminase- mediated, heat-induced porcine myofibrillar protein gel: Effect of salt level and transglutaminase incubation. Meat Sci. 81, 565-572. https://doi.org/10.1016/j.meatsci.2008.10.012
  8. Dybowska, B. E. and Fujio, Y. (1998) Optical properties of the pre-gel and gel state of soy proteins gelled by GdL under different physical conditions. J. Food Eng. 35, 471-482. https://doi.org/10.1016/S0260-8774(98)00038-7
  9. Feng, J. and Xiong, Y. L. (2002) Interaction of myofibrillar and preheated soy proteins. J. Food Sci. 67, 2851-2856. https://doi.org/10.1111/j.1365-2621.2002.tb08827.x
  10. Hamm, R. (1986) Functional properties of the myofibrillar system and their measurements. In: Muscle as food. Bechtel, P. J. (ed) Academic Press, Inc., FL, pp. 135-199.
  11. Hayashi, R., Kawamura, Y., Nakasa, T., and Okinaka, O. (1989) Application of high pressure to food processing: pressurization of egg white and yolk, and properties of gels formed. Agric. Biol. Chem. 53, 2935-2939. https://doi.org/10.1271/bbb1961.53.2935
  12. Hong, G. P., Park, S. H., Kim, J. Y., and Min, S. G. (2006) The effects of high pressure and various binders on the physico- chemical properties of restructured pork meat. Asian- Aust. J. Anim. Sci. 19, 1484-1489. https://doi.org/10.5713/ajas.2006.1484
  13. Hong, G. P., Ko, S. H., Choi, M. J., and Min, S. G. (2008) Effect of glucono-$\delta$-lactone and $\kappa$-carrageenan combined with high pressure treatment on the physico-chemical properties of restructured pork. Meat Sci. 79, 236-243. https://doi.org/10.1016/j.meatsci.2007.09.007
  14. Ichikawa, T. and Shimomura, M. (2007) Effects of sodium chloride and other salts on the properties of diluted egg white sols and gels. Food Sci. Technol. Res. 13, 173-177. https://doi.org/10.3136/fstr.13.173
  15. Jiang, J., Xiong, Y. L., and Chen, J. (2010) pH shifting alters solubility characteristics and thermal stability of soy protein isolate and its globulin fractions in different pH, salt concentration, and temperature conditions. J. Agric. Food Chem. 58, 8035-8042. https://doi.org/10.1021/jf101045b
  16. Jung, S., Ghoul, M., and de Lamballerie-Anton, M. (2003) Influence of high pressure on the color and microbial quality of beef meat. Lebensm. Wiss. u. Technol. 36, 625-631. https://doi.org/10.1016/S0023-6438(03)00082-3
  17. Knorr, D., Heinz, V., and Buckow, R. (2006) High pressure application for food biopolymers. Biochim. Biophys. Acta. 1764, 619-631. https://doi.org/10.1016/j.bbapap.2006.01.017
  18. Kuraishi, C., Sakamoto, J., Yamazaki, K., Susa, Y., Kuhara, C., and Soeda, T. (1997) Production of restructured meat using microbial transglutaminase without salt or cooking. J. Food Sci. 62, 488-490. https://doi.org/10.1111/j.1365-2621.1997.tb04412.x
  19. Lucey, J. A., van Vliet, T., Grolle, K., Geurts, T., and Walstra, P. (1997) Properties of acid casein gels made by acidification with glucono-$\delta$-lactone. 1. Rheological properties. Int. Dairy J. 7, 381-388. https://doi.org/10.1016/S0958-6946(97)00027-7
  20. Lucey, J. A. and Horne, D. S. (2009) Milk salts: Technological significance. In: Advanced dairy chemistry. Lactose, water, salts and minor constituents (Vol. 3). McSweeney, P. L. H. and Fox, P. F. (eds) Springer, NY, pp. 351-390.
  21. Messens, W., Van Camp, J., and Huyghebaert, A. (1997) The use of high pressure to modify the functionality of food proteins. Trend. Food Sci. Technol. 8, 107-112. https://doi.org/10.1016/S0924-2244(97)01015-7
  22. Ngapo, T. M., Wilkinson, B. H. P., and Chong, R. (1996) 1,5- Glucono-$\delta$-lactone-induced gelation of myofibrillar protein at chilled temperatures. Meat Sci. 42, 3-13. https://doi.org/10.1016/0309-1740(95)00028-3
  23. Pelegrine, D. H. G. and Gasparetto, C. A. (2005) Whey proteins solubility as function of temperature and pH. Lebensm. Wiss. u. Technol. 38, 77-80. https://doi.org/10.1016/j.lwt.2004.03.013
  24. Roesch, R., Juneja, M., Monagle, C., and Corredig, M. (2004) Aggregation of soy/milk mixes during acidification. Food Res. Int. 37, 209-215. https://doi.org/10.1016/j.foodres.2003.11.003
  25. Shen, J. L. (1976) Solubility profile, intrinsic viscosity, and optical rotation studies of acid precipitated soy protein and of commercial soy isolate. J. Agric. Food Chem. 24, 784-788. https://doi.org/10.1021/jf60206a044
  26. Vasbinder, A. J., van de Velde, F., and de Kruif, C. G. (2004) Gelation of casein-whey protein mixtures. J. Dairy Sci. 87, 1167-1176. https://doi.org/10.3168/jds.S0022-0302(04)73265-8
  27. Visschers, R. W. and de Jongh, H. H. J. (2005) Disulphide bond formation in food protein aggregation and gelation. Biotechnol. Adv. 23, 75-80. https://doi.org/10.1016/j.biotechadv.2004.09.005
  28. Weijers, M., van de Velde, F., Stijnman, A., van de Pijpekamp, A., and Visschers, R. W. (2006) Structure and rheological properties of acid-induced egg white protein gels. Food Hydrocolloid. 20, 146-159. https://doi.org/10.1016/j.foodhyd.2005.02.013
  29. Xiong, Y. L. (2000) Protein oxidation and implications for muscle food quality (Chapter 4). In: Antioxidants in muscle foods: Nutritional strategies to improve quality. Decker, E. A., Faustman, C., and Lopez-Bote, C. J. (eds) John Wiley & Sons, Inc., NY, pp. 85-111.

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