$\require{mediawiki-texvc}$
  • 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
안녕하세요!
ScienceON 챗봇입니다.
궁금한 것은 저에게 물어봐주세요.

논문 상세정보

Abstract

The purpose of this study was performed as model study using four animals to investigate the correction between the changes in Differential Scanning Calorimetry thermogram of muscle proteins during storage and meat freshness. M. longissimus dorsi of pork was obtained immediately after slaughter and chilled/stored at either $-2^{\circ}C$ or $25^{\circ}C$ for up to 96 h for analyses. DSC thermograms were determined and compared with pH values, ATP-related compounds, K-values, volatile basic nitrogen (VBN) levels, bacterial counts and electrophoretic behavior. Changes in pH, bacterial counts, VBN and K-values were associated with increased storage temperature and time. The levels of pH values, bacterial counts, VBN and K-values of pork samples stored at $25^{\circ}C$ were higher than those of the pork samples stored at $-2^{\circ}C$. ATP concentration decreased faster in samples stored at $25^{\circ}C$. Only IMP increased in samples stored at $-2^{\circ}C$, whereas the concentration of hypoxanthine and inosine increased in samples stored at $25^{\circ}C$. One exothermic peak and two endothermic peaks appeared on the thermograms of pork stored at either temperature. Lower transition temperature of myosin, sarcoplasmic protein and actin peaks were observed. The freshness parameters of K-value, VBN and hypoxanthine showed highly negative correlations (-0.742- -0.9980) to the changes in transition temperature. Therefore, the shift temperature on DSC thermogram can be used as an indicator of the freshness parameters of meat.

참고문헌 (30)

  1. Boyle, J. L., R. C. Lindsay and D. A. Stuiber. 1991. Adenosine nucleotide degradation in modified atmosphere chill-stored fresh fish. J. Food Sci. 56:1267-1270. 
  2. Chen, M. T. and S. L. Guo. 1992a. Studies on the microbial flora of Chinese-style sausage. 2. Action of selected organisms isolated from Chinese-style sausage on porcine muscle proteins. Fleischwirt. 72:1126-1128. 
  3. Hamm, R. 1981. Postmortem changes in muscle affecting the quality of comminuted meat products. In 'Developments in Meat Sci. 2.' (Ed. R. Lawrie) Appl. Sci. Pub., Inc., London. 
  4. Kijowski, J. M. and M. G. Mast. 1988. Thermal properties of proteins in chicken broiler tissues. J. Food Sci. 53:363-366. 
  5. Okuma, H. and E. Watanabe. 2002. Flow system for fish freshness determination based on double multi-enzyme reactor electrodes. Biosensor and Bioelectronics 17:367-372. 
  6. Park, J. W. and T. C. Lanier. 1988. Calorimetric changes during development of rigor mortis. J. Food Sci. 53:1312-1314, 1372. 
  7. Saito, T. K. Ara and M. Matsuyoshi. 1959. A new method for estimating the freshness of fish. Bul. Japan. Soc. Sci. Fish 24:249-250. 
  8. Watanable, A., H. Sato, E. Tsuneishi, M. Matsumoto and Y. Takimoto. 1992. Effect of slaughter methods on the postmortem changes of pH and ATP-related compounds of beef muscles. Jpn. Anim. Sci. Technol. 63:935-941. 
  9. Hwang, I. H. and J. M. Thompson. 2002. A technique to quantify the extent postmortem degradation of meat ultrastructure. Asian-Aust. J. Anim. Sci. 15:111-116. 
  10. Cannon, J. E., J. B. Morgan, J. Heavner, F. K. McKeith, G. C. Smith and D. L. Meeker. 1995. Pork quality audit: A review of the factors influencing pork quality. J. Muscle foods. 6:369-402. 
  11. Chen, M. T., C. P. Lee and D. C. Liu. 1992b. Studies on 2, 3- Diphosphoglycerate, pyruvate kinase and mitochondrial ATPase activities in PSS pig. Proceeding of 38th International Cong. Meat Sci. Technol. 3:345-346. 
  12. Judge, M. D., E. D. Aberle, J. C. Forrest, H. B. Hedrick and R. A. Merkel. 1989. Principles of meat science. 2nd edition Kendall. pp. 85-133. Hunt pub. Co. 
  13. Hofmann, K. 1988. pH a quality criterion for meat. Fleischwirt. 68:67-70. 
  14. Jensen, K. N. and B. M. Jorgensen. 2003. Effect of storage conditions on differential scanning calorimetry profiles from thawed cod muscle. Lebensm-Wiss. U. Technol. 36:807-812. 
  15. Ryder, J. M. 1985. Determination of ATP and its breakdown products in fish muscle by high-performance liquid chromatography. J. Agric. Food Chem. 33:678-680. 
  16. Wagner, J. R. and M. C. Anon. 1985. Denaturation kinetics of myofibrillar proteins in bovine muscle. J. Food Sci. 50:1547-1550. 
  17. Wright, D. J., I. B. Leach and P. Wilding. 1977. DSCC studies of muscle and its constituent proteins. J. Sci. Food Agric. 28:577-564. 
  18. Ehira, S. 1976. A biochemical study on the freshness of fish. Bull. Tokai. Reg. Fish Res. Labor. 88:1-132. 
  19. Stabursvik, E. and H. Martens. 1980. Thermal denaturation of proteins in post-rigor muscle tissue as studies by differential scanning calorimetry. J. Sci. Food Agric. 31:1034-1042. 
  20. Xiang, Y. L. and C. J. Brekke. 1990. Thermal transitions of salt soluble proteins from pre- and post-rigor chicken muscles. J. Food Sci. 55:1540-1543. 
  21. Kimura, I. O., S. M. Sugimoto and T. O. Fujita. 1987. Measurement of fish flesh freshness by DSC. Netsu Sokutei. 14:37-38. Japan. 
  22. Goodno, C. C. and C. A. Swenson. 1975. Thermal transitions of myosin and its helical fragments. II. Solvent-induced variations in conformational stability. Biochem. 14:873-878. 
  23. Samejima, K., M. Ishioroshi and T. Yasui. 1983. Scanning calorimetric studies on the thermal denaturation of myosin and its subfragments. Agric. Biol. Chem. 47:2373-2379. 
  24. AOAC. 1984. Official methods of Analysis, 14th ed., Association of Official American Chemists. Washington. DC. USA. 
  25. SAS. 1995. SAS system for window 95 (Release 6.111). SAS Inst. Inc., Cary, USA. 
  26. Stabursvik, E., K. Fretheim and T. Frostein. 1984. Myosin denaturation in pale, soft and exudative (PSE) porcine muscle tissue as studies by differential scanning calorimetry. J. Sci. Food Agric. 35:240-244. 
  27. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 277:680-685. 
  28. Chen, M. T., C. P. Lee and D. C. Liu. 1992. DSC Studies on thermal properties of muscle proteins in normal and PSE pork. Proceedings of 38th International Cong. Meat Sci. Technol. 3:347-350. France. 
  29. Food and Drug Administration. 1975. FDA Bacteriological Analytical Manual for Food. 4th ed., FDA, Washington, DC. USA. 
  30. Barbut, S. and C. J. Findlay. 1991. Influence of sodium, potassium and magnesium chloride on thermal properties of beef muscles. J. Food Sci. 56:180-182. 

이 논문을 인용한 문헌 (0)

  1. 이 논문을 인용한 문헌 없음

원문보기

원문 PDF 다운로드

  • ScienceON :
  • KCI :

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