메뉴 건너뛰기




Volumn 32, Issue 5, 1999, Pages 261-268

The Effect of Freeze-Thawing on the Magnetic Resonance Imaging Parameters of Cod and Mackerel

Author keywords

Authentication; Cod; Fish; Frozen storage; Mackerel; MRI; Quality

Indexed keywords

GADUS MORHUA; SCOMBER SCOMBRUS;

EID: 0242651517     PISSN: 00236438     EISSN: None     Source Type: Journal    
DOI: 10.1006/fstl.1999.0549     Document Type: Article
Times cited : (30)

References (35)
  • 2
    • 0001946355 scopus 로고
    • Preservation of seafood quality
    • F. SHAHIDI, BOTTA J. R. London: Blackie Academic and Professional
    • SIKORSKI Z. E., SUN PAN B. Preservation of seafood quality. SHAHIDI F., BOTTA J. R. Seafoods: chemistry, processing technology and quality. 1994;168-195 Blackie Academic and Professional, London.
    • (1994) Seafoods: Chemistry, Processing Technology and Quality , pp. 168-195
    • Sikorski, Z.E.1    Sun Pan, B.2
  • 3
    • 0008422651 scopus 로고
    • Fish Muscle as Food
    • BECHTEL P. J. London: Academic Press
    • BROWN W. D. Fish Muscle as Food. BECHTEL P. J. Muscle as Food. 1986;405-451 Academic Press, London.
    • (1986) Muscle As Food , pp. 405-451
    • Brown, W.D.1
  • 4
    • 0031318949 scopus 로고    scopus 로고
    • Authentication of the effect of freezing/thawing of pork by quantitative magnetic resonance imaging
    • GUIHENEUF T. M., PARKER A. D., TESSIER J. J., HALL L. D. Authentication of the effect of freezing/thawing of pork by quantitative magnetic resonance imaging. Magnetic Resonance in Chemistry. 35:1997;S112-S118.
    • (1997) Magnetic Resonance in Chemistry , vol.35
    • Guiheneuf, T.M.1    Parker, A.D.2    Tessier, J.J.3    Hall, L.D.4
  • 5
    • 0032276097 scopus 로고    scopus 로고
    • The effect of freezing and thawing on the magnetic resonance imaging parameters of water in beef, lamb and pork meat
    • EVANS S. D., NOTT K. P., KSHIRSAGAR A., HALL L. D. The effect of freezing and thawing on the magnetic resonance imaging parameters of water in beef, lamb and pork meat. International Journal of Food Science and Technology. 33:1998;317-328.
    • (1998) International Journal of Food Science and Technology , vol.33 , pp. 317-328
    • Evans, S.D.1    Nott, K.P.2    Kshirsagar, A.3    Hall, L.D.4
  • 6
    • 84948501135 scopus 로고
    • The effects of freezing on flesh proteins
    • MACKIE I. M. The effects of freezing on flesh proteins. Food Reviews International. 9:1993;575-610.
    • (1993) Food Reviews International , vol.9 , pp. 575-610
    • Mackie, I.M.1
  • 7
    • 0032945096 scopus 로고    scopus 로고
    • Quantitative magnetic resonance imaging of fresh and frozen-thawed trout
    • NOTT K. P., EVANS S. D., HALL L. D. Quantitative magnetic resonance imaging of fresh and frozen-thawed trout. Magnetic Resonance Imaging. 17:1999;445-455.
    • (1999) Magnetic Resonance Imaging , vol.17 , pp. 445-455
    • Nott, K.P.1    Evans, S.D.2    Hall, L.D.3
  • 8
    • 0029828560 scopus 로고    scopus 로고
    • High-resolution NMR and magnetic resonance imaging (MRI) studies on fresh and frozen cod (Gadus morhua) and haddock (Melanogrammus aeglefinus)
    • HOWELL N. K., SHAVILLA Y., GROOTVELD M., WILLIAMS S. High-resolution NMR and magnetic resonance imaging (MRI) studies on fresh and frozen cod (Gadus morhua) and haddock (Melanogrammus aeglefinus). Journal of the Science of Food and Agriculture. 72:1996;49-56.
    • (1996) Journal of the Science of Food and Agriculture , vol.72 , pp. 49-56
    • Howell, N.K.1    Shavilla, Y.2    Grootveld, M.3    Williams, S.4
  • 9
    • 84988106424 scopus 로고
    • Beta hydroxylacyl CoA dehydrogenase (HADH) differentiates unfrozen from frozen-thawed crawfish (Procambarus clarkii) and trout (Salmo gairdneri)
    • HOZ L., YUSTES C., CAMARA J. M., RAMOS M. A., DE FERNANDO G. D. G. Beta hydroxylacyl CoA dehydrogenase (HADH) differentiates unfrozen from frozen-thawed crawfish (Procambarus clarkii) and trout (Salmo gairdneri). International Journal of Food Science and Technology. 27:1992;133-136.
    • (1992) International Journal of Food Science and Technology , vol.27 , pp. 133-136
    • Hoz, L.1    Yustes, C.2    Camara, J.M.3    Ramos, M.A.4    De Fernando, G.D.G.5
  • 10
    • 0027279996 scopus 로고
    • Differentiation of unfrozen and frozen-thawed kuruma prawn (Penaeus japonicus) from the activity of beta hydroxylacyl CoA dehydrogenase (HADH) in aqueous extracts
    • HOZ L., FERNADEZ M., DIAZ O., ORDONEZ J. A., PAVLOV A., DE FERNANDO G. D. G. Differentiation of unfrozen and frozen-thawed kuruma prawn (Penaeus japonicus) from the activity of beta hydroxylacyl CoA dehydrogenase (HADH) in aqueous extracts. Food Chemistry. 48:1993;127-129.
    • (1993) Food Chemistry , vol.48 , pp. 127-129
    • Hoz, L.1    Fernadez, M.2    Diaz, O.3    Ordonez, J.A.4    Pavlov, A.5    De Fernando, G.D.G.6
  • 12
    • 0039928216 scopus 로고    scopus 로고
    • Thawed fish - Validity and limits of some analytical techniques and suggestions for their employment
    • CIVERA T., REBUFATTI P., PARISI E. Thawed fish - Validity and limits of some analytical techniques and suggestions for their employment. Industrie Alimentari. 35:1996;813-818.
    • (1996) Industrie Alimentari , vol.35 , pp. 813-818
    • Civera, T.1    Rebufatti, P.2    Parisi, E.3
  • 13
    • 0030776323 scopus 로고    scopus 로고
    • Texture changes in frozen cod mince measured by low-field nuclear magnetic resonance spectroscopy
    • STEEN C., LAMBELET P. Texture changes in frozen cod mince measured by low-field nuclear magnetic resonance spectroscopy. Journal of the Science of Food and Agriculture. 75:1997;268-272.
    • (1997) Journal of the Science of Food and Agriculture , vol.75 , pp. 268-272
    • Steen, C.1    Lambelet, P.2
  • 14
    • 85007974088 scopus 로고
    • Insolubilisation of rainbow trout actomyosin during storage at -20°C. I. Properties of insolubilised proteins formed by reactions of propanal and caproic acid with actomyosin
    • TAKAMA K. Insolubilisation of rainbow trout actomyosin during storage at -20°C. I. Properties of insolubilised proteins formed by reactions of propanal and caproic acid with actomyosin. Bulletin of the Japanese Society of Scientific Fisheries. 40:1974;585-588.
    • (1974) Bulletin of the Japanese Society of Scientific Fisheries , vol.40 , pp. 585-588
    • Takama, K.1
  • 15
    • 85008129546 scopus 로고
    • Changes in the flesh lipids of fish during frozen storage. III. Relation between rancidity in fish flesh and protein extractability
    • TAKAMA K., ZAMA K., IGARASHI H. Changes in the flesh lipids of fish during frozen storage. III. Relation between rancidity in fish flesh and protein extractability. Bulletin of the Japanese Society of Scientific Fisheries. 38:1972;607-612.
    • (1972) Bulletin of the Japanese Society of Scientific Fisheries , vol.38 , pp. 607-612
    • Takama, K.1    Zama, K.2    Igarashi, H.3
  • 18
    • 0031312957 scopus 로고    scopus 로고
    • Efficient magnetic resonance imaging methods for automated quantitation of MR parameters from multiple samples
    • EVANS S. D., NOTT K. P., KSHIRSAGAR A., HALL L. D. Efficient magnetic resonance imaging methods for automated quantitation of MR parameters from multiple samples. Magnetic Resonance in Chemistry. 35:1997;S76-S80.
    • (1997) Magnetic Resonance in Chemistry , vol.35
    • Evans, S.D.1    Nott, K.P.2    Kshirsagar, A.3    Hall, L.D.4
  • 19
    • 0039806141 scopus 로고    scopus 로고
    • Magnetic resonance imaging (MRI) of meat products: 1 - Automated quantitation of the NMR relaxation parameters of cured pork, by 'bulk' and MRI methods
    • GUIHENEUF T. M., TESSIER J. J., HERROD N. J., HALL L. D. Magnetic resonance imaging (MRI) of meat products: 1 - Automated quantitation of the NMR relaxation parameters of cured pork, by 'bulk' and MRI methods. Journal of the Science of Food and Agriculture. 71:1996;163-173.
    • (1996) Journal of the Science of Food and Agriculture , vol.71 , pp. 163-173
    • Guiheneuf, T.M.1    Tessier, J.J.2    Herrod, N.J.3    Hall, L.D.4
  • 20
    • 84985755099 scopus 로고
    • Relaxation time measurements in NMR imaging, Part I: Longitudinal relaxation time
    • KALDOUDI E., WILLIAMS S. C. R. Relaxation time measurements in NMR imaging, Part I: Longitudinal relaxation time. Concepts in Magnetic Resonance. 5:1993;217-242.
    • (1993) Concepts in Magnetic Resonance , vol.5 , pp. 217-242
    • Kaldoudi, E.1    Williams, S.C.R.2
  • 21
  • 24
    • 0024573913 scopus 로고
    • Magnetisation transfer contrast (MTC) and tissue water proton relaxation in vivo
    • WOLFF S. D., BALABAN R. S. Magnetisation transfer contrast (MTC) and tissue water proton relaxation in vivo. Magnetic Resonance in Medicine. 10:1989;135-144.
    • (1989) Magnetic Resonance in Medicine , vol.10 , pp. 135-144
    • Wolff, S.D.1    Balaban, R.S.2
  • 26
    • 0029298410 scopus 로고
    • Interpretation of magnetisation transfer and proton cross-relaxation spectra of biological tissues
    • TESSIER J. J., DILLON N., CARPENTER T. A., HALL L. D. Interpretation of magnetisation transfer and proton cross-relaxation spectra of biological tissues. Journal of Magnetic Resonance Series B. 107:1995;138-144.
    • (1995) Journal of Magnetic Resonance Series B , vol.107 , pp. 138-144
    • Tessier, J.J.1    Dillon, N.2    Carpenter, T.A.3    Hall, L.D.4
  • 28
    • 0021132985 scopus 로고
    • Simple proton spectroscopic imaging
    • DIXON W. T. Simple proton spectroscopic imaging. Radiology. 153:1984;189-194.
    • (1984) Radiology , vol.153 , pp. 189-194
    • Dixon, W.T.1
  • 30
    • 0030444429 scopus 로고    scopus 로고
    • Thawing, refreezing and frozen storage effects on muscle functionality and sensory attributes of frozen cod
    • HURLING R., MCARTHUR H. Thawing, refreezing and frozen storage effects on muscle functionality and sensory attributes of frozen cod. Journal of Food Science. 61:1996;1289-1296.
    • (1996) Journal of Food Science , vol.61 , pp. 1289-1296
    • Hurling, R.1    McArthur, H.2
  • 31
    • 0002120573 scopus 로고
    • Chemical deterioration of muscle proteins during frozen storage
    • MATSUMOTO J. J. Chemical deterioration of muscle proteins during frozen storage. ACS Symposium Series. 123:1980;95-124.
    • (1980) ACS Symposium Series , vol.123 , pp. 95-124
    • Matsumoto, J.J.1
  • 32
    • 0025275876 scopus 로고
    • Quantitative studies of hydrodynamic effects and cross-relaxation in protein solutions and tissues with proton and deuteron longitudinal relaxation times
    • ZHONG J., GORE J. C., ARMITAGE I. M. Quantitative studies of hydrodynamic effects and cross-relaxation in protein solutions and tissues with proton and deuteron longitudinal relaxation times. Magnetic Resonance in Medicine. 13:1990;192-203.
    • (1990) Magnetic Resonance in Medicine , vol.13 , pp. 192-203
    • Zhong, J.1    Gore, J.C.2    Armitage, I.M.3
  • 33
    • 0029361457 scopus 로고
    • Magnetisation transfer in protein solutions at 0.1T: Dependence on concentration, molecular weight, and structure
    • VIRTA A., KOMU M., KORMANO M., LUNDBOM N. Magnetisation transfer in protein solutions at 0.1T: Dependence on concentration, molecular weight, and structure. Academic Radiology. 2:1995;792-798.
    • (1995) Academic Radiology , vol.2 , pp. 792-798
    • Virta, A.1    Komu, M.2    Kormano, M.3    Lundbom, N.4
  • 34
    • 0024345480 scopus 로고
    • 1-weighted images in the differentiation between MS, white matter lesions, and subcortical arteriosclerotic encephalopathy
    • 1-weighted images in the differentiation between MS, white matter lesions, and subcortical arteriosclerotic encephalopathy. Neuroradiology. 31:1989;203-212.
    • (1989) Neuroradiology , vol.31 , pp. 203-212
    • Uhlenbrock, D.1    Sehlen, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.