Quality Characteristics of Chicken Breast Surimi as Affected by Water Washing Time and pH Adjustment



Jin, Sang-Keun;Kim, Il-Suk;Choi, Yeung-Joon;Park, Gu-Boo;Yang, Han-Sul

  • 투고 : 2007.07.28
  • 심사 : 2007.10.10
  • 발행 : 2008.03.01


This study was carried out to compare the quality properties of chicken breast surimi manufactured by four different procedures/methods. Surimi was made from chicken breast by washing two (T1) or four times (T2) with water as well as by pH adjustments at 3.0 (T3) or 11.0 (T4). The contents of moisture and crude fat were significantly higher in the surimi manufactured from pH-adjusted material than after washing. Again, collagen and yield were significantly higher in chicken breast surimi manufactured from washed than pH-adjusted samples, whereas crude protein was higher in the pH-adjusted than washed surimi samples. There was no significant difference in myofibrillar protein content among the surimi manufactured after different washing times and differences following pH adjustments were found. T4 showed highest myofibrillar protein content rating among the surimi samples. All physical characteristics were higher in pH-adjusted chicken breast surimi than in T1 and T2 washed surimi samples. The pH-adjusted surimi had higher hardness, gumminess and chewiness than washed surimi samples (p<0.05). The chicken breast surimi made by pH adjustments had higher lightness (L*) than when made by washing times, whereas pH 3.0-adjusted surimi samples had lower whiteness (W) then the other surimi samples. Myoglobin content was significantly higher in the surimi manufactured from pH-adjusted chicken breast samples.


Surimi;Chicken Breast;Washing Time;pH Adjustment;Gel Properties


  1. Xiong, Y. L. and C. J. Brekke. 1989. Changes in protein solubility and gelation properties of chicken myofibrils during storage. J. Food Sci. 54:1140-1146.
  2. Yang, T. S. and G. W. Froning. 1992. Selected washing processes affect thermal gelation properties and microstructure of mechanically deboned chicken meat. J. Food Sci. 57:325-331. https://doi.org/10.1111/j.1365-2621.1992.tb05486.x
  3. Uddin, M., E. Okazaki, H. Fukushima, S. Turza, Y. Yumiko and Y. Fukuda. 2006. Nondestructive determination of water and protein in surimi by near-infrared spectroscopy. Food Chem. 96:491-495. https://doi.org/10.1016/j.foodchem.2005.04.017
  4. Undeland, I., S. D. Kelleher and H. O. Hultin. 2002. Recovery of functional proteins from herring (Clupea harengus) light muscle by an acid or alkaline solubilization process. J. Agric. Food Chem. 50:7371-7379. https://doi.org/10.1021/jf020199u
  5. Vilhelmsson, O. 1997. The state of enzyme biotechnology in the fish processing industry. Trends in Food Sci. Technol. 8:266- 270. https://doi.org/10.1016/S0924-2244(97)01057-1
  6. Xiong, Y. L. 1997. Structure-function relationships of muscle protein. In: Food proteins and their applications (Ed. S. Damodaran and A. Paraf), Marcel Dekker, NY, USA. pp. 341-392.
  7. Smith, D. M. 1987. Functional and biochemical change in deboned turkey due to frozen storage and lipid oxidation. J. Food Sci. 52:22-27. https://doi.org/10.1111/j.1365-2621.1987.tb13965.x
  8. Smyth, A. B. and E. O'neill. 1997. Heat induced gelation properties of surimi from mechanically separated chicken. J. Food Sci. 62:350-355.
  9. Pearson, A. M. and R. B. Young. 1989. Muscle and meat biochemistry. Academic Press, Inc. New York.
  10. Phatcharat, S., S. Benjakul and W. Visessanguan. 2006. Effects of washing with oxidizing agents on the gel-forming ability and physicochemical properties of surimi produced from bigeye snapper. Food Chem. 98:431-439. https://doi.org/10.1016/j.foodchem.2005.06.016
  11. SAS. 1997. SAS/STAT Software for PC. SAS Institude Inc., Cary, NC, USA.
  12. Park, S., M. S. Brewer, J. Novakofski, P. J. Bechtel and F. K. McKeith. 1996. Process and characteristics for a surimi-like material made from beef or pork. J. Food Sci. 61:422-427. https://doi.org/10.1111/j.1365-2621.1996.tb14208.x
  13. Park, J. D., C. H. Jung, J. S. Kim, D. M. Cho, M. S. Cho and Y. J. Choi. 2003. Surimi processing using acid alkali solubilization of fish muscle protein. J. Kor. Soc. Food Sci. Nutr. 32:400-405. https://doi.org/10.3746/jkfn.2003.32.3.400
  14. Palka, K. 1999. Changes in intramuscular connective tissue and collagen solubility of bovine m.semitendinosus during retorting. Meat Sci. 53:189-194. https://doi.org/10.1016/S0309-1740(99)00047-9
  15. Park, W. J. 1994. Functional protein additives in surimi gel. J. Food Sci. 59:525-527. https://doi.org/10.1111/j.1365-2621.1994.tb05554.x
  16. Lanier, T. C. 2000. Surimi gelation chemistry. In: Surimi and surimi seafood (Ed. J. W. Park). Marcel Dekker, NY, USA. pp. 237-265.
  17. Lee, S. K., J. H. Han, C. G. Kang, M. Lee and B. C. Kim. 1999. Washing solution and cycle affected quality properties of surimi from mechanically deboned chicken meat. Kor. J. Anim. Sci. 41:687-696.
  18. Luo, Y., R. Kuwahara, M. Kaneniwa, Y. Murata and M. Yokoyama. 2004. Effect of soy protein isolate on gel properties of alaska pollack and common carp surimi at different setting conditions. J. Sci. Food Agric. 84:663-671. https://doi.org/10.1002/jsfa.1727
  19. Mizuta, S., K. Nakashima and R. Yoshinaka. 2007. Behaviour of connective tissue in fish surimi on fractionation by sieving. Food Chem. 100:477-481. https://doi.org/10.1016/j.foodchem.2005.09.068
  20. Kang, G. H., H. S. Yang, J. Y. Jeong, S. H. Moon, S. J. Hur, G. B. Park and S. T. Joo. 2007. Gel color and texture of surimi-like pork from muscles at different rigor state post-mortem. Asian-Aust. J. Anim. Sci. 20:1127-1134. https://doi.org/10.5713/ajas.2007.1127
  21. Kristinsson, H. G. and H. O. Hultin. 2003. Role of pH and ionic strength on water relationships in washed minced chicken breast muscle gels. J. Food Sci. 68:917-922. https://doi.org/10.1111/j.1365-2621.2003.tb08265.x
  22. Kuo, J. M. and C. Y. Chu. 2003. Quality characteristics of Chinese sausage made from PSE pork. Meat Sci. 64:441-449. https://doi.org/10.1016/S0309-1740(02)00213-9
  23. Jung, C. H., J. S Kim, S. K. Jin, I. S. Kim, K. J. Jung and Y. J. Choi. 2004. Gelation properties and industrial application of functional protein from fish muscle-2. Properties of functional protein gel from fish, chicken breast and pork leg and optimum formulation. J. Kor. Soc. Food Sci. Nutr. 33:1676-1684. https://doi.org/10.3746/jkfn.2004.33.10.1676
  24. Han-Ching, L. and A. Leinot. 1993. Surimi composition and technology: present status and nutritional consideration. Int. J. Food Sci. Nutr. 44(S1):S55-S63. https://doi.org/10.3109/09637489309017423
  25. Hastings, R. J., J. N. Keay and K. W. Young. 1990. The properties of surimi and kamaboko gels made nine British species of fish. Int. J. Food Sci. Technol. 25:281-294.
  26. Jin, S. K., I. S. Kim, S. J. Kim, K. J. Jeong, Y. J. Choi and S. J. Hur. 2007. Effect of muscle type and washing times on physicochemical characteristics and quality of surimi. J. Food engine. 81:618-623. https://doi.org/10.1016/j.jfoodeng.2007.01.001
  27. Choi, Y. J. and J. W. Park. 2000. Feasibility study of new acidaided surimi processing methods for enzyme-laden Pacific whiting. Institute of Food Technologist. Dallas, TX, USA.
  28. Clark, J. M., Jr. and R. L. Switzer. 1977. Experimental biochemistry. Sanfrancisco: W. H. Freeman & Company.
  29. Gomez-Basauri, J. V. and J. F. Regenstein. 1992. Vacuum package, ascorbic acid and frozen storage effect on heme and nonheme iron content of mackerel. J. Food Sci. 57:1337-1339 https://doi.org/10.1111/j.1365-2621.1992.tb06851.x
  30. Hamann, D. D. 1988. Rheology as a means of evaluating functionality in processing muscle foods. Food Technol. 42:66-71.
  31. Bourne, M. C. 1978. Texture profile analysis. Food Technol. 32:62-66, 72.
  32. Chaijan, M., S. Benjakul, W. Visessanguan and C. Faustman. 2004. Characteristics and gel properties of muscles from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) caught in Thailand. Food Res. Int. 37:1021-1030. https://doi.org/10.1016/j.foodres.2004.06.012
  33. Chen, H. H. 2002. Decoloration and gel-forming ability of horse mackerel mince by air-flotation washing. J. Food Sci. 67:2970- 2975. https://doi.org/10.1111/j.1365-2621.2002.tb08847.x
  34. AOAC. 2000. Official method of analysis (15th ed). Arlington, VA: Association of Official Analytical Chemists.
  35. Baker, R. C. and C. A. Bruce. 1989. Further processing of poultry. In: Processing poultry (Ed. G. C. Mead). Elsevier Science Publishers Ltd, London and NY. pp. 251-282.
  36. Yang, T. S. and G. W. Froning. 1990. Study of protein solubility during the washing of mechanically deboned chicken meat. Poul. Sci. 69:147 (Abstr.).
  37. Lin, T. M. and J. W. Park. 1996. Extraction of proteins from Pacific whiting mince at various washing conditions. J. Food Sci. 61:432-438. https://doi.org/10.1111/j.1365-2621.1996.tb14210.x
  38. Yang, H. S., S. S. Moon, J. Y. Jeong, S. G. Choi, S. T. Joo and G. B. Park. 2006. Effect of sodium bicarbonate injection in pre-rigor procine M. Longissimus lumborum on pork quality. Asian-Aust. J. Anim. Sci. 19:898-904. https://doi.org/10.5713/ajas.2006.898

피인용 문헌

  1. 1. Alternatives for Efficient and Sustainable Production of Surimi: A Review vol.8, pp.4, 2009, doi:10.5713/ajas.2008.70424
  2. 2. Comparisons of the Properties of Whitemouth Croaker (<i>Micropogonias furnieri</i>) Surimi and Mechanically Deboned Chicken Meat Surimi-Like Material vol.03, pp.11, 2012, doi:10.5713/ajas.2008.70424
  3. 3. Optimization of parameters for obtaining surimi-like material from mechanically separated chicken meat using response surface methodology vol.52, pp.2, 2015, doi:10.5713/ajas.2008.70424
  4. 4. Properties of Frankfurter-type Sausages with Pork Back-fat Replaced with Bovine Heart Surimi-like Materials vol.36, pp.4, 2016, doi:10.5713/ajas.2008.70424


연구 과제 주관 기관 : ministry of agriculture and forestry