Journal of the Korean Society of Food Science and Nutrition (한국식품영양과학회지)

The Korean Society of Food Science and Nutrition (한국식품영양과학회)
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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

기능성 어육단백질의 젤화 특성과 산업적 응용-2. 알칼리 공정으로 회수한 어육, 닭고기 가슴살 및 돼지 후지 육 기능성 단백질 젤의 특성과 최적화

  • 정춘희 (경상대학교 해양생물이용학부/해양산업연구소) ;
  • 김진수 (경상대학교 해양생물이용학부/해양산업연구소) ;
  • 진상근 (국립진주산업대학교 동물소재공학과) ;
  • 김일석 (국립진주산업 대학교 동물소재공학과) ;
  • 정규진 (남도대학 식품공학과) ;
  • 최영준 (경상대학교 해양생물이용학부/해양산업연구소)
  • Published : 2004.12.01
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Abstract

Gel properties of recovered protein from mackerel, frozen blackspotted croaker, chicken breast and pork leg using acidic and alkaline processing were evaluated. Myofibrillar protein from mackerel by acidic processing did not form a heat-induced gel. However, the recovered protein including sarcoplasmic protein formed heatinduced gel. Breaking force of gel from mackerel processed at pH 10.5 was the lowest. A deformation value of frozen blackspotted croaker was the highest, followed by chicken breast, pork leg and mackerel. Whiteness of frozen blackspotted croaker was the highest among heat-induced gel. Breaking force, deformation and whiteness were decreased by addition of recovered protein from mackerel, but price was increased. A breaking force and whiteness of heat-induced gel added recovered protein from chicken breast were increased, and the price was greatly decreased. When the constraint of breaking force, deformation and price of raw material were set up above 110 g, 4.5 mm and below 2,000 won/kg. A optimum formulation for blending protein was 36∼50% for frozen blackspotted croaker, 34∼40% for chicken breast, 14∼25% for pork leg. The heat-induced gel of recovered protein from frozen blackspotted croaker showed compact structure compared to that of recovered protein from mackerel. A formulation of chicken breast and pork leg based on blackspotted croaker can be used in surimi based seafood products having various texture.

어육, 닭 가슴살 및 돼지 후지 육을 산성 및 알칼리 용액으로 추출하여 등전점 부근에서 회수하고 중성 부근의 pH로 재조절하여 회수한 단백질의 가열 젤 물성과 이들의 혼합에 따른 가열 물성 값의 변화, 최적 물성과 최소비용을 제공하는 혼합 비율을 결정하였다. 갈고등어의 근원섬유단백질은 산 및 알칼리 처리에 의해 가열 젤을 형성하지 못하였으나, 산과 알칼리 처리후 근형질 단백질을 포함한 회수 단백질은 가열 젤을 형성하였다. pH 10.5에서 처리 후 회수한 단백질의 가열 젤의 파괴강도는 갈고등어가 가장 낮았고, 변형 값은 냉동 꼬마민어>닭 가슴살>돼지 후지 육>갈고등어의 순으로 높았으며, 백색도는 냉동 꼬마민어 회수 단백질이 가장 높았다. 갈고등어 회수 단백질의 첨가는 파괴강도, 변형 값, 백색도를 감소시키고 가격을 상승시키는 반면, 닭 가슴살 회수 단백질의 첨가는 파괴 강도와 백 색도를 다소 증가시키고 가격을 현저히 감소시켰다. 냉동 꼬마민어 회수 단백질인 경우, 파괴강도 110 g 이상, 변형 값 4.5 mm 이상 및 회수 단백질의 원료 단가 2000원 이하/kg을 만족하는 최적 혼합 비율은 냉동 꼬마민어 36∼50%, 닭 가슴살 34∼40%, 돼지 후지 육 14∼25%이었다 가열 젤의 구조는 냉동 꼬마민어 회수 단백질이 가장 치밀하였다. 냉동 꼬마민어 회수 단백질을 축으로 닭 가슴살, 돼지 후지 육 회수 단백질의 적절한 혼합 비율의 조절은 물성 값이 다양화한 연제품에 활용 가능할 것으로 판단된다.

Keywords

References

  1. Riley C. 2002. Surimi market changes in supply and demand. The 4th OSU surimi Technology School, November 4-6, Amari Atrium Hotel, Bangkok
  2. Morrissey MT, Tan S-M. 2000. World resources for surimi. In Surimi and Surimi Seafood. Park JW, ed. Marcel Dekker, New York. p 1-21
  3. FAO. 2002. 2001 capture production with respect to the previous year. www.fao.org/fisheries
  4. Davis N. 1988. Fatty fish utilization: upgrading from feed to food. UNC Sea Grant Publication 88-04, Raleigh, NC, USA
  5. Jiang S-T, Ho M-L, Jiang S-H, Lo L, Chen H-C. 1998. Color and quality of mackerel surimi as affected by alkaline washing and ozonation. J Food Sci 63: 652-655 https://doi.org/10.1111/j.1365-2621.1998.tb15805.x
  6. Hultin HO, Kelleher SD. 2000. Surimi processing from dark muscle fish. In Surimi and Surimi Seafood. Park JW, ed. Marcel Dekker, New York. p 59-77
  7. Underland I, Kelleher SD, Hultin HO. 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
  8. MacDonald GA, Lelievre J, Wilson NDC. 1992. Effect of frozen storage on the gel-forming properties of hoki (Macruronus novaezelandiae). J Food Sci 57: 69-71 https://doi.org/10.1111/j.1365-2621.1992.tb05427.x
  9. Simpson R, Kolbe E, MacDonald G, Lanier TC, Morrissey M. 1994. Surimi production from partially processed and frozen Pacific whiting (Merluccius productus). J Food Sci 59: 272-276 https://doi.org/10.1111/j.1365-2621.1994.tb06946.x
  10. Park JW, Lin TM, Yongsawatdigul J. 1997. New developments in manufacturing of surimi and surimi seafood. Food Reviews International 13: 577-610 https://doi.org/10.1080/87559129709541141
  11. Toyoda K, Kimura L, Fujita T, Noguchi SF, Lee CM. 1992. The surimi manufacturing process. In Surimi Technology. Lanier TC, Lee CM, eds. Marcel Dekker, New York. p 79- 112
  12. Park JW, Morrissey MT. 2000. Manufacturing of surimi from light muscle fish. In Surimi and Surimi Seafood. Park JW, ed. Marcel Dekker, New York. p 23-58
  13. Watabe S, Maruyama J, Hashimoto K. 1983. Myofibrillar ATPase activity of mackerel ordinary and dark muscles. Nippon Suisan Gakkaishi 49: 655 https://doi.org/10.2331/suisan.49.655
  14. Shimizu Y, Toyohara H, Lanier TC. 1992. Surimi production from fatty and dark-fleshed fish species. In Surimi Technology. Lanier TC, Lee CM, eds. Marcel Dekker, New York. p 181-207
  15. Venugopal V, Kakatkar A, Bongirwar DR, Karthikeyan M, Mathew S, Shamasundar BA. 2002. Gelation of shark meat under mild acidic 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
  16. Choi YJ, Park JW. 2002. Acid-aided protein recovery from enzyme-rich Pacific whiting. J Food Sci 67: 2962-2969 https://doi.org/10.1111/j.1365-2621.2002.tb08846.x
  17. Dewitt CAM, Gomez G, James JM. 2002. Protein extraction from beef heart using acid solubiliztion. J Food Sci 67: 3335- 3341 https://doi.org/10.1111/j.1365-2621.2002.tb09588.x
  18. Kristinsson HG, Hultin HO. 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
  19. Park JD, Jung C-H, Kin J-S, Cho D-M, Cho MS, Choi YJ. 2003. 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
  20. Park JD, Yoon S-S, Jung CH, Cho MS, Choi YJ. 2003. Effect of sarcoplasmic protein and NaCl on heating gel from fish muscle surimi prepared by acid and alkaline processing. J Korean Soc Food Sci Nutr 32: 567-573 https://doi.org/10.3746/jkfn.2003.32.4.567
  21. 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
  22. Park JW. 1994. Functional protein additives in surimi gels. J Food Sci 59: 525-527 https://doi.org/10.1111/j.1365-2621.1994.tb05554.x
  23. JMP. 2002. Statistics and graphics guide. Version 5.0. SAS Institute, Cary, NC. p 179-209
  24. Hashimoto K. 1976. Light and dark muscle fish-Characteristics of muscle. In Fisheries Series. Nippon Suisan Gakkaishi, ed. Hansungsahusnaggak, Tokyo. Vol 13, p 28-41
  25. Shimizu Y, Nishioka F. 1974. Interactions between horse mackerel actomyosin and sarcoplasmic proteins during heat coagulation. Nippon Suisan Gakkaishi 52: 1821-1827
  26. Okazaki E, Kanna K, Suzuki T. 1986. Effect of sarcoplasmic protein on rheological properties of fish meat gel formed by retort-heating. Nippon Suisan Gakkaishi 52: 1821-1827 https://doi.org/10.2331/suisan.52.1821
  27. Morioka K, Shimizu Y. 1990. Contribution of sarcoplasmic proteins to gel formation of fish meat. Nippon Suisan Gakkaishi 56: 929-933 https://doi.org/10.2331/suisan.56.929
  28. Moriloka K, Shimizu Y. 1993. Relationship between the heat-gelling property and composition of fish sarcoplasmic proteins. Nippon Suisan Gakkaishi 59: 1631 https://doi.org/10.2331/suisan.59.1631
  29. Park JD, Kim J-S, Cho Y-J, Choi J-D, Choi YJ. 2003. 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
  30. Choi J-D, Choi YJ. 2003. Optimum formulation of starch and non-muscle protein for alkali surimi gel from jack mackerel. J Korean Soc Food Sci Nutr 32: 1032-1038 https://doi.org/10.3746/jkfn.2003.32.7.1032

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