알칼리 공정으로 회수한 어육 단백질의 동결 안정성

Frozen Stability of Proteins Recovered from Fish Muscle by Alkaline Processing

  • 허성익 (경상대학교 해양생명과학부) ;
  • 임형수 (경상대학교 해양생명과학부) ;
  • 김종현 (창원대학 식품조리과) ;
  • 최영준 (경상대학교 해양생명과학부)
  • Hur, Sung-Ik (Division of Marine Life Science/Institute of Marine Industry, Gyeongsang National University) ;
  • Lim, Hyeong-Soo (Division of Marine Life Science/Institute of Marine Industry, Gyeongsang National University) ;
  • Kim, Jong-Hyun (Dept. of Food and Nutrition, Changwon College) ;
  • Choi, Yeung-Joon (Division of Marine Life Science/Institute of Marine Industry, Gyeongsang National University)
  • 발행 : 2006.08.30


전갱이 회수단백질은 동결저장 기간이 경과함에 따라 잔여지질의 산화생성물도 크게 증가하였으며, 백조기와 전갱이 회수단백질의 갈변도는 저장 90일 이후에 크게 증가하였다. 일반세균의 수는 전갱이 회수단백질이 백조기 회수단백질에 비하여 높았으나, 시판 수리미에서 검출되는 생균수와 거의 일치하였다. 백조기 회수단백질 가열 젤의 파괴강도, 변형 값 및 백색도 값은 저장 120일까지 큰 변화를 보이지 않은 반면, 120일동안 동결저장한 전갱이 회수단백질은 가열 젤을 형성하지 못했다. 가열 젤 형성능과 파괴강도 및 변형 값에 미루어 수산가공을 위한 중간소재로서 백조기와 전갱이 회수단백질의 동결저장 한계는 안정성을 고려할 때 각각 90일과 60일이 적당할 것으로 예측하였다.


  1. Nishiya K, Takeda F, Tamoto K, Tanaka O, Kubo T. 1960. Studies on freezing of surimi (fish paste) and its application. III. Influence of salts on quality of fish meat. Monthly Report of Hokkaido Fisheries Research Laboratory (Fisheries Agency, Japan) 17: 373-383
  2. Carvajal PA, Lanier TC, MacDonald GA. 2004. Stabilization of proteins in surimi. In Surimi and Surimi Seafood. Park JW, ed. Taylor & Francis Inc, New York. p 164-225
  3. Lanier TC, MacDonald GA. 1991. Carbohydrates as cryoprotectants for meats and surimi. Food Technology 45: 150-159
  4. Matsumoto I, Nakakuki T. 1992. Preventive effect of various sugars against denaturation of carp myofibrillar protein caused by freeze-drying. Nippon Suisan Gakkaishi 58: 1913-1918
  5. 新井健一. 2000. 水産食品と糖アルコール. 東和化成工業株式會社, 富士市, 日本. p 56-63
  6. Matsumoto I, Arai KI. 1987. Cooperative effect of carboxylic acid and sugar against freeze denaturation of fish myofibrillar protein. Nippon Suisan Gakkaishi 53: 2187-2193
  7. Nielsen RG, Pigott GM. 1994. Gel strength increased low-grade heat-stable surimi with blended phosphates. J Food Sci 59: 246-250
  8. Carpenter JF, Arakawa T, Crowe JH. 1991. Interactions of stabilizing additives with proteins during freeze-thawing and freeze-drying. Develop Biol Standard 74: 225-239
  9. Sotelo CG, Rehbein H. TMAO-degrading enzymes. In Seafood Enzymes. Haard NF, Simpson BK, eds. Marcel Dekker Inc., New York. p 167-190
  10. Choi YJ, Park JD, Kim JS, Cho YJ, Park JW. 2002. Rheological properties of heat-induced gels of surimi from acid and alkali process. J Korean Fish Soc 35: 309-314
  11. Kim YS, Park JW, Choi YJ. 2003. New approach for the effective recovery of fish proteins and their physicochemical characteristics. Fisheries Science 69: 1231-1239
  12. Choi YJ, Park JW. 2002. Acid-aided protein recovery from enzyme-rich Pacific whiting. J Food Sci 67: 2962-2967
  13. Scott DN, Porter RW, Kudo G, Miller R, Koury B. 1988. Effect of freezing and frozen storage of Alaska pollack on the chemical and gel-forming properties of surimi. J Food Sci 53: 353-358
  14. Katoh N, Nozaki H, Komatsu K, Arai KI. 1979. A new method for evaluation of the quality of frozen surimi from Alaska pollack relationship between myofibrillar ATPase activity and Kamaboko forming ability of frozen surimi. Bull Japan Soc Sci Fish 45: 1027-1032
  15. Wrolstad RE, Acree TE, Decker EA, Penner MH, Reid DS, Schwartz SJ, Shoemaker CF, Smith DM, Sporns P. 2005. Handbook of Food Analytical Chemistry. Wiley-Interscience, NJ. p 548-550
  16. Hirano T, Suzuki T, Suyama M. 1987. Changes in extractive components of bigeye tuna and Pacific halibut meats by thermal processing at high temperature of Fo values of 8 to 21. Nippon Suisan Gakkaishi 53: 1457-1461
  17. Swanson KMJ, Busta FF, Peterson EH, Johnson MG. 1992. Colony count methods. In Compendium of Methods for the Microbiological Examination of Foods. Vanderzant C, Splittstoesser DF, eds. American Public Heath Association, MI. p 75-95
  18. Okada M. 1964. Effect of washing on the jelly forming ability of fish meat. Bull Japan Soc Sci Fish 30: 255-261
  19. Park JW. 1995. Surimi gel colors as affected by moisture content and physical conditions. J Food Sci 60: 15-18
  20. SAS Institute. 2002. JMP Statistics and graphics guide. SAS Institute Inc, Cary, NC. p 88-121
  21. Sikorski Z, Olley J, Kostuch S. 1976. Protein changes in frozen fish. Crit Rev Food Sci Nutr 8: 97-129
  22. Richards MP, Hultin HO. 2003. Hemolysates from mackerel, herring and trout promote lipid oxidation at different rates. Fisheries Science 69: 1298-1300
  23. Choi YJ. 2004. New process for recovery of fish protein using pH shift. Ministry of Maritime Affairs & Fisheries, Seoul, Korea
  24. Undeland I, Kristinson HG, Hultin HO. 2004. Hemoglobin- mediated oxidation of washed minced cod muscle phospholipids: Effect of pH and hemoglobin source. J Agric Food Chem 52: 4444-4451
  25. Lee KH, Cho TY, Cho HS, Lee JH, Shim KH. 1998. Lipid oxidation in shellfish under the different conditions of drying. J Korean Fish Soc 31: 143-148
  26. Lee JS. 1992. Microbiological considerations in surimi manufacturing. In Surimi Technology. Lanier TC, Lee CM, eds. Marcel Dekker Inc, New York. p 113-121
  27. Kim D-P. 1985. Bacterial quality of fish meat paste products and isolation of thermoduric bacteria. MS Thesis. National Fisheries University of Pusan. p 38-39
  28. Elliot EL. 1987. Microbiological quality of Alaska pollock surimi. In Seafood Quality Determination. Kramer DE, Liston J, eds. Elsevier, Amsterdam. p 269-281
  29. Kim BY, Park JW, Yoon WB. 2004. Rheology and texture properties of surimi gels. In Surimi and Surimi Seafood. Park JW, ed. Taylor & Francis, New York. p 491-582