• 검색어에 아래의 연산자를 사용하시면 더 정확한 검색결과를 얻을 수 있습니다.
  • 검색연산자
검색연산자 기능 검색시 예
() 우선순위가 가장 높은 연산자 예1) (나노 (기계 | machine))
공백 두 개의 검색어(식)을 모두 포함하고 있는 문서 검색 예1) (나노 기계)
예2) 나노 장영실
| 두 개의 검색어(식) 중 하나 이상 포함하고 있는 문서 검색 예1) (줄기세포 | 면역)
예2) 줄기세포 | 장영실
! NOT 이후에 있는 검색어가 포함된 문서는 제외 예1) (황금 !백금)
예2) !image
* 검색어의 *란에 0개 이상의 임의의 문자가 포함된 문서 검색 예) semi*
"" 따옴표 내의 구문과 완전히 일치하는 문서만 검색 예) "Transform and Quantization"
쳇봇 이모티콘
ScienceON 챗봇입니다.
궁금한 것은 저에게 물어봐주세요.

논문 상세정보

Optimal Conditions for the Distribution of Cryoprotectant into the Intact Fish Muscle of Oncorhynchus mykiss during Freeze/Thaw Cycling


Conditions for sufficient and rapid distribution of a cryoprotectant (sorbitol solution) into intact fish muscle (Oncorhynchus mykiss) were studied as changing in the residual Ca2+ ATPase activity during freeze/thaw cycling. Chunks of the fish muscle were immersed in 4 concentrations of sorbitol solutions ($20\%$, $30\%$, $45\%$, and $60\%$) by a shaker mechanism at 5$^${circ}C. Whole immersion samples (W) showed a higher value of the residual Ca2+ ATPase activity than those in the untreated controls (C), except in the treated controls (TC), while less effect of immersion concentration could be found. Comparing the extent of penetration of sorbitol into the surface layer to inner layer of immersed fish chunks, outer portion samples achieved excellent cryoprotection with $100\%$ of the residual ATPase activity values or more. For the inner portion samples, $30\%$ and $45\%$ sorbitol solution treatments indicated a higher ATPase activity than $60\%$ treatment. At high concentrations, mass transfer rates during osmotic dehydration might berapid and it causes faster surface drying by dewatering at surface solute layer. Periodically immersed and relaxed samples, W (5-3-1), led to good cryoprotection effect: W (5-3-1) indicated high residual Ca2+ ATPase activity values and the residual ATPase activity values excess $100\%$ in immersion of $30\%$ and $45\%$ sorbitol solutions.

참고문헌 (30)

  1. Arakawa, T. and S.N. Timasheff. 1982. Stabilization of protein structure by sugars. Biochemistry, 21, 6536-6544 
  2. Back, J.F., D. Oakenfull and M.B. Smith. 1979. Increased thermal stability of proteins in the presence of sugars and polyols. Biochemistry, 18, 5191-5196 
  3. Bolin. H.R., C.C. Huxsoll, R. Jackson and K.C. Ng. 1983. Effect of osmotic agents and concentration on fruit quality. J. Food Sci., 48, 202-205 
  4. Carpenter, J.F. and J.H. Crowe. 1988. The mechanism of cryoprotection of proteins by solutes. Cryobiology, 25, 244-255 
  5. Carvajal, P.A., G.A. MacDonald and T.C. Lanier. 1999. Cryostabilization mechanism of fish muscle proteins by maltodextrins. Cryobiology, 38, 16-26 
  6. Connell, J.J. 1961. The relative stabilities of the skeletal muscle myosins of some animals. Biochem. J., 80, 503-509 
  7. Fiskke, C.H. and Y. Subbarow. 1925. The colorimetric determination of phosphorus. J. Biol. Chem., 66, 375-400 
  8. Franks. F., J.R. Ravenhill and D.S. Reid. 1972. Thermodynamic studies of dilute aqueous solutions of cyclic ethers and simple carbohydrates. J. Sol. Chem., 1, 3 
  9. Fukuda, Y., Z. Tarakita and K. Arai. 1984. Effect of freshness of chub mackerel on the freeze denaturation of myofibrillar protein. Bull. Jap. Soc. Sci. Fish., 50, 845-852 
  10. Haard, N.F.1992. Biochemical reactions in fish muscle during frozen storage. In: Seafood Science and Technology. Bligh, E.G., ed. Fishing New Books, Oxford, pp. 176-209 
  11. Hashimoto, A., A. Kobayashi and K. Arai. 1982. Thermostability of fish myofibrillar Ca-ATPase and adaptation to environmental temperature. Bull. Jap. Soc. Sci. Fish., 48, 671-684 
  12. Kawashima, T., K. Arai and T. Saito. 1973. Studies on muscular proteins of fish-IX. An attempt on quantitative determination of actomyosin in frozen 'surimi' from Alaska pollack. Bull. Jap. Soc. Sci. Fish., 39, 207-214 
  13. Lee, J.C. and S.N. Timasheff. 1981. The stabilization of proteins by sucrose. J. Biol. Chem., 256, 7193-7201 
  14. MacDonard, G.A., N.D.C. Wilson and T.C. Lanier. 1990. Stabilized mince: an alternative to the traditional surimi process. In: Chilling and Freezing of New Fish Products. Intl, Inst. Refrig., 69-76 
  15. MacDonard, G.A. and T.C. Lanier. 1994. Actomyosin stabilization to freeze-thaw and heat denaturation by lactate salts. J. Food Sci., 59, 101-105 
  16. MacDonald, G.A., T.C. Lanier, H.E. Swaisgood and D.D. Hamann. 1996. Mechnism for stabilization of fish actomyosin by sodium lactate. J. Agr. Food Chem., 44, 106-112 
  17. Matsumoto, J.J. 1979. Denaturation of fish muscle proteins during frozen storage. In: Proteins at Low Temperature, Fennema, O., ed. American Chemical Society, Washington DC, pp. 206-224 
  18. Matsumoto, J.J. and S. Noguchi. 1992. Cryostabilization of protein in Surimi. In: Surimi Technology, Lanier, T.C. and C.M. Lee, cds. Marcel Dekker, Inc., New York, pp. 357-388 
  19. Niwa, E. 1992. The chemistry of surimi gelation. In: Surimi Technology, Lanier, T.C. and C.M. Lee, eds. Marcel Dekker, Inc., New York, pp. 389-428 
  20. Noguchi, S. 1974. The control of denaturation of fish muscle proteins during frozen storage. Ph.D. Thesis, Sophia University, Tokyo, Japan, pp. 138 
  21. Noguchi, S. and J.J. Matsumoto. 1975. Studies on the control of the denaturation of the fish muscle proteins during frozen storage. IV. Preventive effect of carboxylic acids. Bull. Jap. Soc. Sci. Fish., 41, 329-335 
  22. Okada, M. 1992. History of surimi technology in Japan. In: Surimi Technology, Lanier, T.C. and C.M. Lee, eds. Marcel Dekkar, Inc., New York, Dekker, New York, pp. 3-22 
  23. Park, J.W., T.C. Lanier and D.P. Green. 1988. Cryoprotective effects of sugars, polyols, and/or phosphates on Alaska pollock surimi. J. Food Sci., 53, 1-3 
  24. Rastogi, N.K., A. Angersbach and D. Knorr. 2000. Evaluation of mass transfer mechanisms during osmostic trearment of plant materials. J. Food Sci., 65, 1016-1019 
  25. Salvatori, D., A. Andres, A. Albors, A. Chiralt and P. Fito. 1998. Structural and compositional profiles in osmotically dehydrated apple. J. Food Sci., 63, 606-610 
  26. Sych, J., C. Lacroix, L.T. Adambounou and F. Castigne. 1991a. The effect of low- or non-sweet additives on the stability of protein functional properties of frozen cod. Int. J. Food Sci. Technol., 26, 185-197 
  27. Sych, J., C. Lacroix and M. Carrier. 1991b. Determination of optimal level of lactitol for surimi. J. Food Sci., 56, 285-290 
  28. Uedeira, H. 1980. The effect of sugars on the thermal denaturation of lysozyme. Bull. Chem. Soc. Jap., 532, 2451-2455 
  29. Noguchi, S. and J.J. Matsmoto. 1970. Studies on the control of the denaturation of the fish muscle proteins during frozen storage. I. Preventive effect of Na-glutamate. Bull. Jap. Soc. Sci. Fish., 36, 1078-1087 
  30. Tait, M.J., A. Suggett, F. Franks, S. Ablett and P.A. Quickenden. 1972. Hydration of monosaccharides: a study by dielectric and nuclear magnetic relaxation. J. Sol. Chem., 1, 131-151 

이 논문을 인용한 문헌 (0)

  1. 이 논문을 인용한 문헌 없음


원문 PDF 다운로드

  • ScienceON :

원문 URL 링크

원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다. (원문복사서비스 안내 바로 가기)

상세조회 0건 원문조회 0건

DOI 인용 스타일