DOI QR코드

DOI QR Code

돈육 뒷다리부위와 닭가슴살을 활용하여 제조한 수리미의 특성에 미치는 pH 조절의 영향

Effects of pH Adjustment on Characteristics of Surimi Using Pork Leg and Chicken Breast.

  • 진상근 (진주산업대학교 동물소재공학과) ;
  • 김일석 (진주산업대학교 동물소재공학과) ;
  • 양한술 (경상대학교 응용생명과학부) ;
  • 박구부 (경상대학교 응용생명과학부) ;
  • 최영준 (경상대학교 해양생물이용학부) ;
  • 신택순 (부산대학교 동물생명과학과) ;
  • 김병균 (한성식품(주))
  • Jin, Sang-Keun (Department of Animal Resources Technology, Jinju National University) ;
  • Kim, Il-Suk (Department of Animal Resources Technology, Jinju National University) ;
  • Yang, Han-Sul (Division of Applied Life Science, Gyeongsang National University) ;
  • Park, Gu-Boo (Division of Applied Life Science, Gyeongsang National University) ;
  • Choi, Yeung-Joon (Bioscience and Institute of Marine Industry, Gyeongsang National University) ;
  • Shin, Taek-Soon (Department of Animal Life & Resource Science, Busan National University) ;
  • Kim, Byeong-Gyun (Hansung Foods Co., Ltd.)
  • 발행 : 2007.05.25

초록

원료육(돈육 뒷다리 및 닭가슴살)에 따라 pH 조절법(3.0 또는 11.0)으로 제조한 수리미의 이화학적 및 관능적 특성을 비교 분석한 결과, 돈육 뒷다리를 활용한 pH 3.0으로 조절한 수리미는 높은 조단백질 함량, 수율, 보수력을 보였으나, 적색도, 황색도, Mb 및 metMb 함량이 높고(P<0.05) 백색도, 근원섬유단백질, 파괴강도, 변형값 및 겔강도가 낮아(P<0.05) 품질에 나쁜 영향을 미쳤다. 돈육 뒷다리를 활용한 pH 11.0으로 조절한 수리미는 높은 조직 특성과 낮은 Mb 및 metMb 함량으로 인해 양호한 결과를 얻었으나, 가열감량이 낮고 파괴강도, 변형값 및 겔강도가 낮게 나타났다(P<0.05). 또한 닭가슴살을 활용한 pH 3.0으로 조절한 수리미는 높은 조단백질 함량, 수율, pH, 파괴강도, 변형값, 겔강도 및 명도를 보여 양호한 결과를 얻었으나(P<0.05), 근원섬유단백질, 적색도 및 metMb 함량이 높고 수리미의 조직 특성이 낮아 품질에 나쁜 영향을 미쳤다(P<0.05). 닭가슴살을 활용한 pH 11.0으로 조절한 수리미는 근원섬유단백질, 변형 값, 명도, 백색도 및 응집성이 높고 Mb 함량, 가열감량, 조단백질 함량, 수율 및 파괴강도 값이 낮게 나타났다(P<0.05). 따라서 색 및 겔 특성을 기준으로 수리미의 품질 특성을 비교하면, 돈육 뒷다리에 비해 닭가슴살의 활용이 명도, 백색도, 파괴강도, 변형값 및 겔강도 값이 높게 나타났으며, pH 3.0에 비해 pH 11.0으로 회수한 수리미에서 높은 백색도, 근원섬유단백질 함량 및 응집성을 보였다. 그러나 모든 수리미 샘플의 관능평가 항목에서 유의적인 차이가 나타나지 않아, 돈육 뒷다리 및 닭가슴살을 활용한 pH 조절법으로 회수한 수리미의 제조가 가능할 것으로 판단된다..

In this study, we prepared surimi from pork leg and chicken breast by pH adjustments of 3.0 and 11.0. The content of crude protein, yield, water-holding capacity, redness, yellowness, myoglobin(Mb) and metmyoglobin(metMb) were significantly higher in the surimi manufactured from pork leg at adjustment pH 3.0 compared to the other surimi samples; whereas whiteness, myofibrillar protein, breaking force, deformation and gel strength were lower than other samples(P<0.05). The textural attributes were significantly higher in the surimi manufactured from pork leg at adjustment pH 11.0 compared to the other surimi samples; whereas Mb, metMb, cooking loss, breaking force, deformation and gel strength were lower than other samples(P<0.05). Again, the content of crude protein, yield, pH, breaking force, deformation, gel strength and lightness were significantly higher in the surimi manufactured from chicken breast at adjustment pH 3.0 compared to the other surimi samples; whereas myofibrillar protein, redness and metMb were higher than other samples(P<0.05). The content of myofibrillar protein, deformation, lightness and cohesiveness were significantly higher in the suriml manufactured from chicken breast at adjustment pH 11.0 compared to the other surimi samples; whereas Mb, cooking loss, yield and breaking force were higher than other samples(P<0.05). The chicken breast surimi had superior color and gel characteristics than manufactured from pork leg, and adjustment pH 11.0 had superior whiteness and cohesiveness than the pH 3.0 adjusted sample, however, there were no significant differences in sensory attributes among the surimi samples.

키워드

참고문헌

  1. Antonomanolaki, R. E., K. P. Vareltzis, S. A. Georgakis and E. Kaldrymidou. 1999. Thermal gelation properties of surimi-like material made from sheep meat. Meat Sci. 35, 429-435
  2. AOAC. 1990. Official method of analysis, 15th edition. Association of Official Analytical Chemist., Washington, DC
  3. 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
  4. Choi, Y. J. and Y. J. Choi. 1999. Optimization of ingredients formulation in low grades surimi for improvement of gel strength. J. Kor. Fish Sco. 32, 556-562
  5. Clark, J. M., Jr., and R. L. Switzer. 1977. Experimental biochemistry. Sanfrancisco: W. H. Freeman & Company
  6. Ha, J. U. and D. K. Woo. 1997. Water holding capacity, cooking loss and gel characteristics of pork heart surimi prepared by washing under antioxidative condition. Kor. J. Food Sci. Ani. Resour. 17, 226-231
  7. Jin, S. K., I. S. Kim, D. H. Kim, K. J. Jeong and Y. J. Choi. 2006. Comparision of yield, physico-chemical and sensory characteristics for chicken surimi manufactured by alkaline adjustment with different raw materials. Kor. J. Food Sci. Ani. Resour. 26, 431-440
  8. Jin, S. K., . S. Kim, S. J. Kim, K. J. Jeong, Y. J. Choi and S. J. Hur. 2007. Effect of muscle type and washing times on physico-chemical characteristics and quality of surimi. J. Food engineer. 81, 618-623 https://doi.org/10.1016/j.jfoodeng.2007.01.001
  9. Joo, S. T., R. G. Kauffman, B. C. Kim and G. B. Park. 1999. TI1e 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
  10. 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
  11. Knight, M. K. 1992. Red meat and poultly surimi. The Chemistry of Muscle Based Food, pp. 222, In Johnston, D. E., M. K. Knight and D. A. Ledward (eds.), The Royal Society of Chemistry, U. K
  12. 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
  13. Lee, C. M. 1984. Surimi process technology. Food Technol. 38, 69-80
  14. Lee, S. K. and J. H. Han. 1999. Effects of washing temperature and pH on the quality of surimi from mechanically deboned chicken meat. Kor. J. Food Sci. 19, 268-277
  15. 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 de boned chicken meat. Kor. J. Ani.l Sci. 41, 687-696
  16. 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 Agri. 84, 663-671 https://doi.org/10.1002/jsfa.1727
  17. NFI. 1991. A manual of standard methods for measuring and specifying the properties of surimi. Lanier, T. C., Hart, K., Martin, R. E. (Eds.). University of North Carolina Sea Grant College Program, Raleigh, NC, USA
  18. Nowsad, A. A. K. M., S. Kanohand and E. Niwa 2000. Thermal gelation characteristics of breast and thigh muscles of spent hen and broiler and their surimi. Meat Sci. 54, 169-175 https://doi.org/10.1016/S0309-1740(99)00091-1
  19. Oehiai, Y., L. Ochiai, K. Hashimoto and S. Watabe. 2001. Quantitative estimation of dark muscle content in the mackerel meat paste and its productions using antisera against myosin light chains. J. Food Sci. 66, 1301-1305 https://doi.org/10.1111/j.1365-2621.2001.tb15205.x
  20. 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
  21. 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
  22. Park, J. W. and M. T. Morrissey. 2000. Manufacturing of surimi from light muscle fish. pp. 23-58, In Park, J. W. (ed.), Surimi and surimi seafood, Marcel Dekker, New York
  23. Park, J. D., C. H. Jung, J. S. Kim, D. M. Cho, M. S. Cho and Y. J. Choi. 2003a. Surimi processing using acid alkali solubilization of fish muscle protein. J. Korean Soc. Food Sci. Nutr. 32, 400-405 https://doi.org/10.3746/jkfn.2003.32.3.400
  24. Park, J. D., J. S. Kim, Y. J. Cho, J. D. Choi and Y. J. Choi. 2003b. Optimum formulation of starch and non-muscle protein for alkali surimi gel from frozen white croaker. J. Korean Soc. Food Sci. Nutr. 32, 1026-1031 https://doi.org/10.3746/jkfn.2003.32.7.1026
  25. SAS. 1999. SAS/STAT Software for PC. Release 6.11, SAS Institute Inc., Cary, NC, USA
  26. Smyth, A. B. and E. O'neill. 1997. Heat induced gelation properties of surimi from mechanically separated chicken. J. Food Sci. 62, 350-355
  27. 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
  28. Venugopal, V., A. Kakatkar, D. R. Bongirwar, M. Karthikeyan, S. Mathew and B. A. Shamasunder 2002. Gelation of shark meat under mild scidic conditions: Physicochemical and rheological characterization of the gel. J. Food Sci. 67, 2681-2686 https://doi.org/10.1111/j.1365-2621.2002.tb08798.x
  29. Woessner, J. F. 1961. The determination of hydroxyproline in tissue and protein samples containing small proportions of this amino acid. 119 Arch. Biochem. Biophys. 93, 440-447 https://doi.org/10.1016/0003-9861(61)90291-0

피인용 문헌

  1. Effect of Cryoprotectants on the Quality Characteristics of Chicken Breast Surimi Manufactured by pH Adjustment during Freezing Storage vol.27, pp.3, 2007, https://doi.org/10.5851/kosfa.2007.27.3.320
  2. Effect of Cordyceps ochraceostromat, Silkworm Cocoon, and Conjugated Linoleic Acid on the Quality and Storage Characteristics of Pork Sausage Manufactured by MDCM (Mechanically Deboned Chicken Meat) Recovered Protein vol.30, pp.2, 2010, https://doi.org/10.5851/kosfa.2010.30.2.243
  3. Physiochemical properties of pork jerky supplemented with ginger and ginseng powders during curing vol.49, pp.4, 2015, https://doi.org/10.14397/jals.2015.49.4.173