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Effect of Cryoprotectants on Quality Properties of Chicken Breast Surimi

냉동변성방지제의 종류가 닭가슴살 수리미의 품질 특성에 미치는 영향

  • Jin, S.K. (Department of Animal Resources Technology, Jinju National University) ;
  • Kim, I.S. (Department of Animal Resources Technology, Jinju National University) ;
  • Kim, S.J. (Department of Animal Resources Technology, Jinju National University) ;
  • Jeong, K.J. (Department of Animal Resources Technology, Jinju National University) ;
  • Lee, J.R. (Department of Animal Resources Technology, Jinju National University) ;
  • Choi, Y.J. (Division of Marine Bioscience, Gyeongsang National University)
  • 진상근 (진주산업대학교 동물소재공학과) ;
  • 김일석 (진주산업대학교 동물소재공학과) ;
  • 김수정 (진주산업대학교 동물소재공학과) ;
  • 정기종 (진주산업대학교 동물소재공학과) ;
  • 이제룡 (진주산업대학교 동물소재공학과) ;
  • 최영준 (경상대학교 해양생물이용학부)
  • Published : 2007.12.31

Abstract

This study was conducted to determine the effect of cryoprotectants(sugar, sorbitol, polyphosphate) on quality properties of chicken breast surimi manufactured by pH adjustment(pH 11.0) during frozen storage. Final surimi was divided into experimental units to which the following treatments were randomly assigned: C(Alaska pollack surimi, two times washing, 4% sugar+5% sorbitol+0.3% polyphosphate additive); T1(chicken breast surimi, 0.3% polyphosphate additive); T2(chicken breast surimi, 5% sorbitol +0.3% polyphosphate additive); T3(chicken breast surimi, 4% sugar+5% sorbitol+0.3% polyphosphate additive). All amino acid contents of control were higher than those of all treatments, while T2 was higher in amino acid contents among the treatments. Shear force of all treatments were higher than that of control, but the breaking force, deformation and gel strength were lower. The TBARS(thiobarbituric acid reactive substances) and VBN(volatile basic nitrogen) values of all treatments were lower than those of control, The TBARS values of all treatments were increased with increased storage period. In sensory evaluation, the score of appearance, meat color and overall acceptability of control were higher than those of all treatments, but aroma, juiciness and tenderness were lower than those for all treatments.

냉동변성 방지제가 닭가슴살 수리미의 품질 특성에 미치는 영향을 파악하기 위하여 대조구는 2회 수세한 명태수리미를 활용하여 C(4% 설탕+5% 솔비톨+0.3% 인산염 첨가), 나머지 처리구들은 pH(11.0) 조절법으로 제조한 닭가슴살 수리미를 활용하여 T1(0.3% 인산염 첨가), T2(5% 솔비톨+0.3% 인산염 첨가) 및 T3(4% 설탕+5% 솔비톨+0.3% 인산염 첨가) 처리구로 하여 시험한 결과를 요약하면 다음과 같다. 대조구가 처리구들에 비해 모든 아미노산, FAA, SAAA, FRAA, EAA 및 총 아미노산 함량이 높았고, 처리구 간에는 T2 처리구가 T1과 T3 처리구에 비해 높은 함량을 보였다. 전단가는 모든 처리구들이 대조구에 비해 현저하게 높았고, 처리구 간에는 T2 처리구가 T1와 T3 처리구에 비해 높았다. 파괴강도, 변형값 및 겔강도는 대조구가 모든 처리구들에 비해 높았다. 저장기간 동안 모든 처리구의 TBARS값은 0.09~0.48mg/100g으로 대조구의 1.57~1.97mg/ 100g에 비해 현저하게 낮았고, 처리구 간에는 T2 처리구가 가장 낮은 값을 나타내었다. VBN값은 모든 처리구들이 대조구에 비해 낮았다. 관능평가에서 외관, 육색 및 전체적 기호도는 대조구가 모든 처리구들에 비해 높은 점수를 받았지만, 풍미, 다즙성 및 연도는 모든 처리구들이 대조구에 비해 높은 점수를 받았다. 냉동변성제와 닭가슴살을 이용한 수리미는 어육 수리미에 비해 외관과 전체적 기호도 점수가 낮았지만, 조직감, TBARS 및 VBN 값이 낮아 좀 더 연구가 이루어진다면 부가가치가 있는 제품 개발 가능성이 있는 것으로 판단된다.

Keywords

References

  1. AOAC. 1990. Official methods of analysis, 15th edition, Association Official Analytical Chemists, Washington, DC. p. 931
  2. Baily, M. E. 1983. The Maillard reaction and meat flavor. In the Maillard in food and nutrition. Waller G. R., Feather M. S., eds. American Chemical Society, Washington DC, p. 169
  3. Brewer, M. S., Ikins, W. G. and Harbers, C. A. Z. 1992. TBA values, sensory characteristics and volatiles in ground pork during long-term frozen storage: Effects of packaging. J. Food Sci. 57: 558-562 https://doi.org/10.1111/j.1365-2621.1992.tb08042.x
  4. Buege, J. A. and Aust, J. D. 1978. Microsomal lipid peroxidation. Methods Enzymol. 52:302-309 https://doi.org/10.1016/S0076-6879(78)52032-6
  5. Chae, H. S., Cho, S. H., Park, B. Y., Yoo, Y. M., Kim, J. H., Ahn, C. N., Lee, J. M, Kim, Y. K. and Choi, Y. I. 2002. Changes of the Fatty Acid, Amino Acids and collagen Contents in Domestic Broiler Chickens of Different Marketing Standard. Kor. J. Food Sci. Ani. Resour. 22:1-7
  6. Chen, T, C. and Wailmaleongoraek, C. 1981. Effect of pH on TBA values of ground raw poultry meat. J. Food Sci. 46:1946-1958 https://doi.org/10.1111/j.1365-2621.1981.tb04525.x
  7. Chizzolini, R., Novelli, E. and Zanardi, E. 1998. Oxidation in traditional mediterranean meat products. Meat Sci. 49:87-99 https://doi.org/10.1016/S0309-1740(98)90040-7
  8. Decker, E. A., Chan, W. K. M., Livisay, S. A., Butterfield, D. A. and Faustman, C. 1995. Interaction between camosine and the different redox states of myoglobin. J. Food Sci. 60:1201-1204 https://doi.org/10.1111/j.1365-2621.1995.tb04555.x
  9. Decker, E. A., Xiong, Y. L., Calvert, J. T., Crumb, A. D. and Blanchard, S. P. 1993. Chemical, physical and functional properties of oxidized turkey white muscle myofibrillar proteins. J. Agric. Food Chem., 41.186-192 https://doi.org/10.1021/jf00026a007
  10. Ha, J. U. and Woo, D. K. 1997. Water holding capacity, cooking loss and gel characteristics of pork heart surimi prepared by washings under antioxidative condition. Kor. J. Food Sci. Ani. Resour. 17:226-2317
  11. Jin, S. K., Kim, I. S., Hur, S. J., Park, K. H., Ha, J. H., Kang, S. M., Choi, Y. J. and Kim, J. S. 2006. Effect of pH control on physico-chemical characteristics of chicken breast surimi. Kor. J. Food Sci. Ani. Resour. 26:64-69
  12. Juliano, C, Cossu, M., Alamanni, M. M. and Piu, L. 2005. Antioxidant activity of gamma-oryzanol: Mechanism of action and its effect on oxidative stability of pharmaceutical oils. International J. Pharma. 299:146-154 https://doi.org/10.1016/j.ijpharm.2005.05.018
  13. Jung, C. H., Kim, J. S., Jin, S. K., Kim, I. S., Jung, K. J. and Choi, Y. J. 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. Kor. J. Soc. Food Sci. Nutr. 33:1676-1684 https://doi.org/10.3746/jkfn.2004.33.10.1676
  14. Kelleher, S. D., Hultin, H. O. and Wilhelm, K. A. 1994. Stability of mackerel surimi prepared under lipid-stabilizing processing conditions. J. Food Sci. 59:269-274 https://doi.org/10.1111/j.1365-2621.1994.tb06945.x
  15. Kristinsson, H. G. and Hultin, H. O. 2003. Role of pH and ionic strength on water relationships in washed min-ced chicken breast muscle gels. J. Food Sci. 68:917-922 https://doi.org/10.1111/j.1365-2621.2003.tb08265.x
  16. Lefebvre, N., Thibault, C, Charbonneau, R. and Piette, J. P. G. 1994. Improvement of shelf-life and wholeso-me-ness of ground beef by irradiation. Meat Sci. 32:371-377
  17. Lin, T. M. and Park, J. W. 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
  18. Mecci, E., Mordente, A. and Martorana, G. E. 1991. Metal catalyzed oxidation of human serum albumin : conformational and functional changes. J. Biol. Chem. 266:4696-4702
  19. Okada, M. 1964. Effect of washing on the jelly forming ability of fish meat. Nippon Suisan Gakkaishi. 30:255-261 https://doi.org/10.2331/suisan.30.255
  20. Park, J. D., Yoon, S. S., Jung, C. H, Cho, M. S. and Choi, Y. J. 2003. Effect of sarcoplasmic protein and NaCl on heating gel from fish muscle surimi prepared by acid and alkaline processing. Kor. J. Soc. Food Sci. 32:567-573 https://doi.org/10.3746/jkfn.2003.32.4.567
  21. Park, J. W., Lanier, T. C. and Green, D. P. 1988. Cryoprotective effects of sugar, polyols and/or phosphates on Alaska pollack surimi. J. Food Sci. 53:1-3 https://doi.org/10.1111/j.1365-2621.1988.tb10163.x
  22. Park, K. H., Jin, S. K., Kim, I. S., Ha, J. H., Kang, S. M., Choi, Y. J. and Kim, J. S. 2005. Physico-chemical characteristics of surimi by washing method and pH control level of chopped chicken breast. J. Anim. Sci. & Technol. (Kor.) 47:1059-1066 https://doi.org/10.5187/JAST.2005.47.6.1059
  23. Pearson, R. C, McKenna, D. R., Ellebracht, J. W., Griffin, D. B., McKeith, F. K., Scanga, J. A., Belk, K. E., Smith, G. C. and Savel, J. W. 2005. Benchmarking value in the pork supply chain: Processing and consumer characteristics of hams manufacture from different quality raw materials. Meat Sci. 70:91-97 https://doi.org/10.1016/j.meatsci.2005.01.001
  24. Ryu, H. S., Lee, K. W. and Lee, K. H. 1994. Effects of processing conditions on nutrition qualities of seafood. 2. Effects of cryoprotectants on the protein qualities of pollock surimi. Bull. Kor. Fish. Soc. 27:335-343
  25. SAS. 1999. SAS/STAT Software for PC. Release 6.11, SAS Institute Inc., Cary, NC, USA
  26. Shin, K. K., Park, H. I., Lee, S. K. and Kim, C. J. 1998. Studies on fatty acid composition of different portions in various meat. Kor. J. Food Sci. Ani. Resour. 18:261-268
  27. Simmhuber, R. O. and Yu, T. C. 1977. The 2-thiobarbituric acid reaction an objective measure of the oxidative deterioration occurring in fats and oil. J. Japan Soc. Fish Sci. 26:259-267
  28. Stadtman, E. R. and Oliver, C. N. 1991. Metal catalyzed oxidation of proteins. J. Biol. Chem. 266:2005-212
  29. Toyoda, K., Kimura, I., Fujita, T., Noguchi, S. F. and Lee, C. M. 1992. The surimi manufacturing process. In Surimi Technology, Lanier, T. C. Lee, C. M. Eds., Dekker, New York, pp. 79-112
  30. Uchida, K., Kato, Y. and Kawakishi, S. 1992. Metal-catalyzed oxidative degradation of collagen. J. Agric. Food Chem. 40:9-16 https://doi.org/10.1021/jf00013a002
  31. Wang, B., Xiong, Y. L. and Srinivasan, S. 1997. Chemical stability of antioxidant washed beef heart surimi during frozen storage. J. Food Sci. 62:939-946 https://doi.org/10.1111/j.1365-2621.1997.tb15011.x
  32. Watabe, S., Maruyama, J. and Hashimoto, K. 1983. Myofibrillar ATPase activity of mackerel ordinary and dark muscles. Nippon Suisan Gakkaishi. 49:655-662 https://doi.org/10.2331/suisan.49.655
  33. Yin, F. S. and Faustman, C. 1993. Influence of temperature, pH and phospholipid composition upon the stability of myoglobin and phospholipid: a liposome model. J. Agr. Food Chem. 41:853-857 https://doi.org/10.1021/jf00030a002
  34. 강창기, 박구부, 성상경, 이무하, 이영현, 정명섭, 최양일. 1994. 식육생산과 가공의 과학. 선진문화사
  35. 高坂和久. 1975. 肉製品の鮮度保持と 測定. 食品工業. 18:105-111
  36. 森高明. 1980. 日本食品工業學會誌. 27. 579

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