Food Science of Animal Resources (한국축산식품학회지)

Korean Society for Food Science of Animal Resources (한국축산식품학회)
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Interactions between Chicken Salt-soluble Meat Proteins and Makgeolli Lees Fiber in Heat-induced Gels

  • Choi, Yun-Sang (Food and Biological Resources Examination Division, Korean Intellectual Property Office) ;
  • Park, Kwoan-Sik (Department of Food Science and Biotechnology of Animal Resources, Konkuk University) ;
  • Kim, Hack-Youn (Department of Food Science and Biotechnology of Animal Resources, Konkuk University) ;
  • Kim, Hyun-Wook (Department of Food Science and Biotechnology of Animal Resources, Konkuk University) ;
  • Song, Dong-Heon (Department of Food Science and Biotechnology of Animal Resources, Konkuk University) ;
  • Chung, Hai-Jung (Department of Food Science and Nutrition, Daejin University) ;
  • Lee, Ju-Woon (Radiation Technology Institute, Korea Atomic Energy Research Institute) ;
  • Kim, Cheon-Jei (Department of Food Science and Biotechnology of Animal Resources, Konkuk University)
  • Received : 2011.09.17
  • Accepted : 2011.10.19
  • Published : 2011.12.31
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Abstract

The technological effects of Makgeolli lees fiber (0, 0.5, 1.0, 2.0, and 4.0%) on chicken salt-soluble breast meat proteins in a model system on proximate composition, physicochemical properties, and textural properties were investigated. Makgeolli lees fiber was obtained from Makgeolli brew processing, and the by-products showed good dietary fiber. The moisture and ash contents, water holding capacity, redness, yellowness, hardness, and apparent viscosity of chicken salt-soluble meat protein heat-induced gel systems with Makgeolli lees fiber were all higher than the control without Makgeolli lees fiber. However, protein solubility and electrophoretic patterns did not differ among the control and treatments with Makgeolli lees fiber samples. The chicken salt-soluble protein heat-induced gel systems incorporating Makgeolli lees fiber had improved water holding capacity, textural properties, and viscosity due to Makgeolli lees fiber addition. These results suggest that the addition of 4.0% Makgeolli lees fiber to gel is helpful to improve the physical properties of heat-induced gels.

Keywords

References

  1. Aktas, N. and Genccelep, H. (2006) Effect of starch type and its modifications on physicochemical properties of bolognatype sausage produced with sheep tail fat. Meat Sci. 74, 404-408. https://doi.org/10.1016/j.meatsci.2006.04.012
  2. AOAC (1995) Official methods of analysis, 16th ed., Association of Official Analytical Chemists, Washington, DC.
  3. Bae, S. H., Jung, E. Y., Kim, S. Y., Shin, K. S., and Suh, H. J. (2010) Antioxidant and immune-modulating activities of Korean traditional rice wine, takju. J. Food Biochem. 34, 233-248. https://doi.org/10.1111/j.1745-4514.2009.00327.x
  4. Blandino, A., Al-Aseeri, M. E., Pandiella, S. S., Cantero, D., and Webb, C. (2003) Cereal-based fermented foods and beverages. Food Res. Int. 36, 527-543. https://doi.org/10.1016/S0963-9969(03)00009-7
  5. Bourne, M. C. (1982) Food texture and viscosity: concept and measurement. Academic Press, NY, pp. 118-167.
  6. Camou, J. P., Sebranek, J. G., and Olson, D. G. (1989) Effect of heating rate and protein concentration on gel strength and water loss of muscle protein gels. J. Food Sci. 54, 850-854. https://doi.org/10.1111/j.1365-2621.1989.tb07897.x
  7. Chin, K. B. (2000) Functional properties of heat-induced gels prepared with salt soluble proteins, non-meat proteins and hydrocolloids in a model system. Food Sci. Biotechnol. 9, 368-371.
  8. Chin, K. B., Keeton, J. T., Longnecker, M. T., and Lamkey, J. W. (1999) Utilization of soy protein isolate and konjac blends in a low-fat bologna (model system). Meat Sci. 53, 45-57. https://doi.org/10.1016/S0309-1740(99)00035-2
  9. Choi, Y. S., Choi, J. H., Han, D. J., Kim, H. Y., Lee, M. A., Kim, H. W., Lee, J. W., Chung, H. J., and Kim, C. J. (2010a) Optimization of replacing pork back fat with grape seed oil and rice bran fiber for reduced-fat meat emulsion systems. Meat Sci. 84, 212-218. https://doi.org/10.1016/j.meatsci.2009.08.048
  10. Choi, Y. S., Choi, J. H., Han, D. J., Kim, H. Y., Lee, M. A., Kim, H. W., Jeong, J. Y., and Kim, C. J. (2011) Effects of rice bran fiber on heat-induced gel prepared with pork salt-soluble meat proteins in model system. Meat Sci. 88, 59-66. https://doi.org/10.1016/j.meatsci.2010.12.003
  11. Choi, Y. S., Choi, J. H., Han, D. J., Kim, H. Y., Lee, M. A., Kim, H. W., and Kim, C. J. (2009) Characteristics of low-fat meat emulsion systems with pork fat replaced by vegetable oils and rice bran fiber. Meat Sci. 82, 266-271. https://doi.org/10.1016/j.meatsci.2009.01.019
  12. Choi, Y. S., Choi, J. H., Han, D. J., Kim, H. Y., Lee, M. A., Lee, E. S., Jeong, J. Y., Paik, H. D., and Kim, C. J. (2008) Effect of rice bran fiber on quality of low-fat tteokgalbi. Food Sci. Biotechnol. 17, 959-964.
  13. Choi, Y. S., Park, K. S., Choi, J. H., Kim, H. W., Song, D. H., Kim, J. M., Chung, H. J., and Kim, C. J. (2010b) Physicochemical properties of chicken meat emulsion systems with dietary fiber extracted from Makgeolli lees. Korean J. Food Sci. Ani. Resour. 30, 910-917. https://doi.org/10.5851/kosfa.2010.30.6.910
  14. Cofrades, S., Lopez-Lopez, I., Solas, M. T., Bravo, L., and Jimenez-Colmenero, F. (2008) Influence of different types and proportions of added edible seaweeds on characteristics of low-salt gel/emulsion meat systems. Meat Sci. 79, 767-776. https://doi.org/10.1016/j.meatsci.2007.11.010
  15. DeFreitas, Z., Sebranek, J. G., Olson, D. G., and Carr, J. M. (1997) Carrageenan effects on salt-soluble meat proteins in model systems. J. Food Sci. 62, 539-543. https://doi.org/10.1111/j.1365-2621.1997.tb04425.x
  16. Farouk, M. M. and Swan, J. E. (1997) Effect of pH at time of salting on the functional properties of pre-rigor beef. Meat Sci. 45, 463-472. https://doi.org/10.1016/S0309-1740(96)00125-8
  17. Farouk, M. M., Wieliczko, K., Lim, R., Turnwald, S., and MacDonald, G. A. (2002) Cooked sausage batter cohesiveness as affected by sarcoplasmic proteins. Meat Sci. 61, 85-90. https://doi.org/10.1016/S0309-1740(01)00168-1
  18. Garcia-Garcia, E. and Totosaus, A. (2008) Low-fat sodiumreduced sausages: Effect of the interaction between locust bean gum, potato starch and ${beta}$-carrageenan by a mixture design approach. Meat Sci. 78, 406-413. https://doi.org/10.1016/j.meatsci.2007.07.003
  19. Gornall, A. G., Bardawill, C. J., and David, M. M. (1949) Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177, 751-766.
  20. Jeong, J. W. and Park, K. J. (2006) Quality characteristics of loaf bread added takju powder. Korean J. Food Sci. Technol. 38, 52-58.
  21. Joo, S. T., Kauffman, R. G., Kim, B. C., and Park, G. B. (1999) The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle. Meat Sci. 52, 291-297. https://doi.org/10.1016/S0309-1740(99)00005-4
  22. Kocher, P. and Foegeding, E. (1993) Microcentrifuge-based method for measuring water-holding of protein gels. J. Food Sci. 58, 1040-1046. https://doi.org/10.1111/j.1365-2621.1993.tb06107.x
  23. Koohmaraie, M., Kennick, W. H., Elgasim, E. A., and Anglemier, A. F. (1984) Effects of postmortem storage on muscle protein degradation: Analysis by SDS-polyacrylamide gel electrophoresis. J. Food Sci. 49, 292-294. https://doi.org/10.1111/j.1365-2621.1984.tb13732.x
  24. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685. https://doi.org/10.1038/227680a0
  25. Lan, Y. H., Novakofski, J., Carr, T. R., and McKeith, F. K. (1993) Assay and storage conditions affect yield of salt-soluble protein from muscle. J. Food Sci. 58, 963-967. https://doi.org/10.1111/j.1365-2621.1993.tb06089.x
  26. Lanier, T. C. (1991) Interactions of muscle and nonmuscle proteins affecting heat-set gel rheology. In: Marcromolecular Interactions and Food Colloid Stability. Parris, N. and Barford, R. A. (eds) American Chemical Society, Symposium Series, Washington, DC, pp. 268-284.
  27. Lanier, T. C., Carvajal, P., and Yongaswatdigul, J. (2004) Surimi gelation chemistry. In: Surimi and surini seafood. 2nd ed, Prak, J. W. (ed) Marcel Dekker, Inc., NY, pp. 451-470.
  28. Lee, J. S., Lee, T. S., Noh, B. S., and Park, S. O. (1996) Quality characteristics of mash of takju prepared by different raw materials. Korean J. Food Sci. Technol. 28, 330-336.
  29. Lee, M. A., Han, D. J., Jeong, J. Y., Choi, J. H., Choi, Y. S., Kim, H. Y., Paik, H. D., and Kim, C. J. (2008) Effect of kimchi powder level and drying methods on quality characteristics of breakfast sausage. Meat Sci. 80, 708-714. https://doi.org/10.1016/j.meatsci.2008.03.010
  30. Liu, R., Zhao, S, M., Xiong, S. B., Xie, B. J., and Qin, L. H. (2008) Role of secondary structures in the gelation of porcine myosin at different pH values. Meat Sci. 80, 632-639. https://doi.org/10.1016/j.meatsci.2008.02.014
  31. McCord, A., Smyth, A., and O'Neill, E. E. (1998) Heat-induced gelation properties of salt-soluble muscle proteins as affected by non-meat proteins. J. Food Sci. 63, 580-583.
  32. Nakayama, T. and Sato, Y. (1971) Relationship between binding quality of meat and myofibrillar protein. J. Texture Stud. 2, 475-488. https://doi.org/10.1111/j.1745-4603.1971.tb00595.x
  33. Nuckles, R. O., Smith, D. M., and Merkel, R. A. (1991) Properties of heat-induced gels from beef skeletal, heart, lung and spleen protein fractions. J. Food Sci. 56, 1165-1170. https://doi.org/10.1111/j.1365-2621.1991.tb04725.x
  34. Osburn, W. N. and Keeton, J. T. (2004) Evaluation of low-fat sausage containing desinewed lamb and konjac gel. Meat Sci. 68, 221-233. https://doi.org/10.1016/j.meatsci.2004.03.001
  35. Park, S. Y., Wang, S. H., Chin, K. B., and Kim, Y. D. (2004) Rheological properties of the mixture and heat-induced gel prepared from pork salt soluble protein in combined with soluble chitooligosaccharide and chitosan. Korean J. Food Sci. Technol. 36, 594-597.
  36. Samejima, K., Yamaguchi, H., Asghar, A., and Yasui, T. (1984) Role of myosin heavy chains from rabbit skeletal muscle in the heat-induced gelation mechanism. Agric. Biol. Chem. 48, 2225-2232. https://doi.org/10.1271/bbb1961.48.2225
  37. SAS (2008) SAS/STAT Software for PC. Release 9.2, SAS Institute Inc., Cary, NC, USA.
  38. Sayre, R. N. and Briskey, E. J. (1963) Protein solubility as influenced by physiological conditions in the muscle. J. Food Sci. 28, 675-679. https://doi.org/10.1111/j.1365-2621.1963.tb01673.x
  39. Smith, D. M. (1998) Meat proteins: Functional properties of comminuted meat products. Food Technol. 42, 116-121.
  40. Verbeken, D., Neirinck, N., Van-Der, M. P., and Dewettinck, K. (2005) Influence of ${beta}$-carrageenan on the thermal gelation of salt-soluble meat proteins. Meat Sci. 70, 161-166. https://doi.org/10.1016/j.meatsci.2004.12.007
  41. Wang, S. F., Smith, D. M., and Steffe, J. F. (1990) Effect of pH on the dynamic rhelogical properties of chicken breast salt-soluble protein during heat-induced gelation. Poultry Sci. 69, 2220-2227. https://doi.org/10.3382/ps.0692220
  42. Weber, K. and Osborn, M. (1969) The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4406-4412.
  43. Westphalen, A. D., Briggs, J. L., and Lonergan, S. M. (2006) Influence of muscle type on rheological properties of porcine myofibrillar protein during heat-induced gelation. Meat Sci. 72, 697-703. https://doi.org/10.1016/j.meatsci.2005.09.021
  44. Xiong, Y. L. (1997) Structure-function relationships of muscle proteins. In: Food proteins and their applications. Damondaran, S. and Paraf, A. (eds) Marcel Dekker, Inc., NY, pp. 341-392.

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