메뉴 건너뛰기




Volumn 47, Issue 3, 1999, Pages 952-959

Structural changes of hake (Merluccius merluccius L.) fillets: Effects of freezing and frozen storage

Author keywords

Freezing; Frozen storage; Functionality; Hake; Protein structure; Raman spectroscopy; Texture

Indexed keywords

PROTEIN;

EID: 0032940822     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf9809481     Document Type: Article
Times cited : (105)

References (46)
  • 1
    • 0001021914 scopus 로고
    • Determination of the quantitative secondary structure of proteins by using some parameters of the Raman amide I band
    • Alix, A. J. P.; Pedanou, G.; Berjot, M. Determination of the quantitative secondary structure of proteins by using some parameters of the Raman amide I band. J. Mol. Struct. 1988, 174, 159-164.
    • (1988) J. Mol. Struct. , vol.174 , pp. 159-164
    • Alix, A.J.P.1    Pedanou, G.2    Berjot, M.3
  • 2
    • 0011807556 scopus 로고
    • Denaturation of cod myosin during freezing after modification with formaldehyde
    • Ang, J. F.; Hultin, H. O. Denaturation of cod myosin during freezing after modification with formaldehyde. J. Food Sci. 1989, 54, 814-818.
    • (1989) J. Food Sci. , vol.54 , pp. 814-818
    • Ang, J.F.1    Hultin, H.O.2
  • 4
    • 0018161217 scopus 로고
    • Laser-Raman light-scattering observations of conformational changes in myosin induced by inorganic salts
    • Barret, T. W.; Peticolas, W. L.; Robson, R. C. Laser-Raman light-scattering observations of conformational changes in myosin induced by inorganic salts. Biophys. J. 1978, 23, 349-358.
    • (1978) Biophys. J. , vol.23 , pp. 349-358
    • Barret, T.W.1    Peticolas, W.L.2    Robson, R.C.3
  • 5
    • 0031786351 scopus 로고    scopus 로고
    • Frozen hake fillets quality as related to texture and viscosity by mechanical methods
    • Barroso, M.; Careche, M.; Barrios, L.; Borderías, A. J. Frozen hake fillets quality as related to texture and viscosity by mechanical methods. J. Food Sci. 1998, 63, 793-796.
    • (1998) J. Food Sci. , vol.63 , pp. 793-796
    • Barroso, M.1    Careche, M.2    Barrios, L.3    Borderías, A.J.4
  • 6
    • 84991124605 scopus 로고
    • Texture analysis of fish fillets and minced fish by both sensory and instrumental methods
    • Borderías, A. J.; Lamúa, M.; Tejada, M. Texture analysis of fish fillets and minced fish by both sensory and instrumental methods. J. Food Technol. 1983, 18, 85-95.
    • (1983) J. Food Technol. , vol.18 , pp. 85-95
    • Borderías, A.J.1    Lamúa, M.2    Tejada, M.3
  • 7
    • 0002841740 scopus 로고
    • Parameters affecting viscosity as a quality control for frozen fish
    • Borderías, A. J.; Jiménez Colmenero, F.; Tejada, M. Parameters affecting viscosity as a quality control for frozen fish. Mar. Fish. Rev. 1985, 47, 43-45.
    • (1985) Mar. Fish. Rev. , vol.47 , pp. 43-45
    • Borderías, A.J.1    Jiménez Colmenero, F.2    Tejada, M.3
  • 9
    • 0031433220 scopus 로고    scopus 로고
    • Structural changes in cod myosin after modification with formaldehyde or frozen storage
    • Careche, M.; Li-Chan, E. C. Y. Structural changes in cod myosin after modification with formaldehyde or frozen storage. J. Food Sci. 1997, 62, 717-723.
    • (1997) J. Food Sci. , vol.62 , pp. 717-723
    • Careche, M.1    Li-Chan, E.C.Y.2
  • 10
    • 0000920106 scopus 로고    scopus 로고
    • Importance of frozen storage temperature in the type of aggregation of myofibrillar proteins in cod (Gadus morhua) fillets
    • Careche, M.; Del Mazo, M. L.; Torrejón, P.; Tejada, M. Importance of frozen storage temperature in the type of aggregation of myofibrillar proteins in cod (Gadus morhua) fillets. J. Agric. Food Chem. 1998, 46, 1539-1546.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 1539-1546
    • Careche, M.1    Del Mazo, M.L.2    Torrejón, P.3    Tejada, M.4
  • 11
    • 0023786443 scopus 로고
    • Conformation of brain proteolipid apoprotein. Effects of sonication and n-octyl-β-D-glucopyranoside detergent
    • Carmona, P.; de Cozar, M.; García-Segura, L. M.; Monreal, J. Conformation of brain proteolipid apoprotein. Effects of sonication and n-octyl-β-D-glucopyranoside detergent. Eur. Biophys. J. 1988, 16, 169-176.
    • (1988) Eur. Biophys. J. , vol.16 , pp. 169-176
    • Carmona, P.1    De Cozar, M.2    García-Segura, L.M.3    Monreal, J.4
  • 12
    • 0016169865 scopus 로고
    • Determination of the helix and β form of proteins in aqueous solution by circular dichroism
    • Chen, Y.-H.; Yang, J. T.; Chau, K. H. Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry 1974, 13, 3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.-H.1    Yang, J.T.2    Chau, K.H.3
  • 13
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton, L. A.; Johnson, W. C., Jr. Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 1986, 155, 155-167.
    • (1986) Anal. Biochem. , vol.155 , pp. 155-167
    • Compton, L.A.1    Johnson W.C., Jr.2
  • 14
    • 84986808912 scopus 로고
    • The role of formaldehyde as a protein cross-linking agent acting during the frozen storage of cod
    • Connell, J. J. The role of formaldehyde as a protein cross-linking agent acting during the frozen storage of cod. J. Sci. Food Agric. 1975, 26, 1925-1929.
    • (1975) J. Sci. Food Agric. , vol.26 , pp. 1925-1929
    • Connell, J.J.1
  • 15
    • 0344299285 scopus 로고    scopus 로고
    • Characteristics of the salt-soluble fraction of hake (Merluccius merluccius) fillets stored at -20 and -30°C
    • in press
    • Del Mazo, M. L.; Torrejón, P.; Careche, M.; Tejada, M. Characteristics of the salt-soluble fraction of hake (Merluccius merluccius) fillets stored at -20 and -30°C. J. Agric. Food Chem. 1999, in press.
    • (1999) J. Agric. Food Chem.
    • Del Mazo, M.L.1    Torrejón, P.2    Careche, M.3    Tejada, M.4
  • 16
    • 0000419395 scopus 로고
    • Protein instability in frozen storage induced in minced muscle of flat fishes by mixture of muscle of red hake
    • Dingle, J. R.; Keith, R. A.; Lall, B. Protein instability in frozen storage induced in minced muscle of flat fishes by mixture of muscle of red hake. Can. Inst. Food Sci. Technol. J. 1977, 10, 143-146.
    • (1977) Can. Inst. Food Sci. Technol. J. , vol.10 , pp. 143-146
    • Dingle, J.R.1    Keith, R.A.2    Lall, B.3
  • 17
    • 0003100933 scopus 로고
    • Raman spectroscopy of proteins
    • Clark, R. J. H., Hester, R. E., Eds.; Heyden: London
    • Frushour, B. G.; Koenig, J. L. Raman spectroscopy of proteins. In Advances in Infrared and Raman Spectroscopy; Clark, R. J. H., Hester, R. E., Eds.; Heyden: London, 1975; Vol. 2, pp 35-97.
    • (1975) Advances in Infrared and Raman Spectroscopy , vol.2 , pp. 35-97
    • Frushour, B.G.1    Koenig, J.L.2
  • 18
    • 84985265255 scopus 로고
    • Textural deterioration of red hake and haddock muscle in frozen storage as related to chemical parameters and changes in the myofibrillar proteins
    • Gill, T. A.; Keith, R. A.; Smith Lall, B.Textural deterioration of red hake and haddock muscle in frozen storage as related to chemical parameters and changes in the myofibrillar proteins. J. Food Sci. 1979, 44, 661-667.
    • (1979) J. Food Sci. , vol.44 , pp. 661-667
    • Gill, T.A.1    Keith, R.A.2    Smith Lall, B.3
  • 19
    • 0002423563 scopus 로고
    • Biochemical reactions in fish muscle during frozen storage
    • Bligh, G., Ed.; Fishing News Books: London, U.K.
    • Haard, N. F. Biochemical reactions in fish muscle during frozen storage. In Seafood Science and Technology; Bligh, G., Ed.; Fishing News Books: London, U.K.; 1990; pp 176-209.
    • (1990) Seafood Science and Technology , pp. 176-209
    • Haard, N.F.1
  • 20
    • 0020487561 scopus 로고
    • Raman spectroscopic study of the interaction between sulfate anion and an imadazolium ring in ribonuclease A
    • Harada, I.; Takamatsu, T.; Tasumi, M.; Lord, R. C. Raman spectroscopic study of the interaction between sulfate anion and an imadazolium ring in ribonuclease A. Biochemestry 1982, 21, 3674-3677.
    • (1982) Biochemestry , vol.21 , pp. 3674-3677
    • Harada, I.1    Takamatsu, T.2    Tasumi, M.3    Lord, R.C.4
  • 21
    • 0023506457 scopus 로고
    • Folding and association of proteins
    • Jaenicke, R. Folding and association of proteins. Prog. Biophys. Mol. Biol. 1987, 49, 117-237.
    • (1987) Prog. Biophys. Mol. Biol. , vol.49 , pp. 117-237
    • Jaenicke, R.1
  • 22
    • 0002632512 scopus 로고
    • The shear press. A device for measuring food quality
    • Kramer, A.; Burkardt, G. J.; Rogers, H. P. The shear press. A device for measuring food quality. Canner 1951, 112, 34.
    • (1951) Canner , vol.112 , pp. 34
    • Kramer, A.1    Burkardt, G.J.2    Rogers, H.P.3
  • 23
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm, S.; Bandekar, J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 1986, 38, 181-365.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-365
    • Krimm, S.1    Bandekar, J.2
  • 24
    • 0011735221 scopus 로고
    • Studies of the changes in the proteins of cod-frame minces during frozen storage at -15°C
    • Advances in Fish Science and Technology; Aberdeen, U.K., 1979; Connell, J. J., staff of Torry Research Station, Eds.; Fishing News Books: Surrey, U.K.
    • Laird, W. M.; Mackie, I. M.; Hattula, T. Studies of the changes in the proteins of cod-frame minces during frozen storage at -15°C. In Advances in Fish Science and Technology; Jubilee Conference of the Torry Research Station, Aberdeen, U.K., 1979; Connell, J. J., staff of Torry Research Station, Eds.; Fishing News Books: Surrey, U.K., 1980; pp 428-434.
    • (1980) Jubilee Conference of the Torry Research Station , pp. 428-434
    • Laird, W.M.1    Mackie, I.M.2    Hattula, T.3
  • 25
    • 0001388698 scopus 로고
    • Raman spectroscopy as a probe of protein structure in food systems
    • Yada, R. Y., Jackman, R. L., Smith, J. L., Eds.; Blackie Academic & Professional, Chapman & Hall: London, U.K.
    • Li-Chan, E.; Nakai, S.; Hirotsuka, M. Raman spectroscopy as a probe of protein structure in food systems. In Protein Structure-Function Relationships in Foods; Yada, R. Y., Jackman, R. L., Smith, J. L., Eds.; Blackie Academic & Professional, Chapman & Hall: London, U.K., 1994; pp 163-197.
    • (1994) Protein Structure-function Relationships in Foods , pp. 163-197
    • Li-Chan, E.1    Nakai, S.2    Hirotsuka, M.3
  • 26
    • 84986517574 scopus 로고
    • Protein insolubilization in frozen Greenland halibut
    • Lim, H.; Haard, N. F. Protein insolubilization in frozen Greenland halibut. J. Food Biochem. 1984, 8, 163-187.
    • (1984) J. Food Biochem. , vol.8 , pp. 163-187
    • Lim, H.1    Haard, N.F.2
  • 27
    • 0017316899 scopus 로고
    • Determination of the secondary structure of proteins by laser Raman spectroscopy
    • Lippert, J. L.; Tyminski, D.; Desmeules, P. J. Determination of the secondary structure of proteins by laser Raman spectroscopy. J. Am. Chem. Soc. 1976, 98, 7075-7080.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 7075-7080
    • Lippert, J.L.1    Tyminski, D.2    Desmeules, P.J.3
  • 29
    • 0022874056 scopus 로고
    • Fluorescence quenching studies of apolipoprotein A-I in solution and in lipid-protein complexes: Protein dynamics
    • Mantulin, W. W.; Pownall, H. J. Fluorescence quenching studies of apolipoprotein A-I in solution and in lipid-protein complexes: protein dynamics. Biochemistry 1986, 25, 8034-8042.
    • (1986) Biochemistry , vol.25 , pp. 8034-8042
    • Mantulin, W.W.1    Pownall, H.J.2
  • 30
    • 0001294231 scopus 로고
    • Denaturation of fish muscle proteins during frozen storage
    • Proteins at Low Temperatures; Fenema, 0., Ed.; American Chemical Society: Washington, DC
    • Matsumoto, J. J. Denaturation of fish muscle proteins during frozen storage. In Proteins at Low Temperatures; Fenema, 0., Ed.; Advances in Chemistry Series 180; American Chemical Society: Washington, DC, 1979; pp 205-224.
    • (1979) Advances in Chemistry Series 180 , vol.180 , pp. 205-224
    • Matsumoto, J.J.1
  • 31
    • 0002120573 scopus 로고
    • Chemical deterioration of muscle proteins during frozen storage
    • Chemical Deterioration of Proteins; Whitaker, J. R., Fujimaki, M., Eds.; American Chemical Society: Washington, DC
    • Matsumoto, J. J. Chemical deterioration of muscle proteins during frozen storage. In Chemical Deterioration of Proteins; Whitaker, J. R., Fujimaki, M., Eds.; ACS Symposium Series 123; American Chemical Society: Washington, DC, 1980; pp 95-124.
    • (1980) ACS Symposium Series 123 , vol.123 , pp. 95-124
    • Matsumoto, J.J.1
  • 32
    • 85008080177 scopus 로고
    • Exposure of hydrophobic amino acid residues from actomyosin on freezing. Reconfirmation by fluorometry
    • Niwa, E.; Kohda, S.; Kanoh, S.; Nakayama, T. Exposure of hydrophobic amino acid residues from actomyosin on freezing. Reconfirmation by fluorometry. Bull. Jpn. Soc. Sci. Fish. 1986, 52, 1039-1042.
    • (1986) Bull. Jpn. Soc. Sci. Fish. , vol.52 , pp. 1039-1042
    • Niwa, E.1    Kohda, S.2    Kanoh, S.3    Nakayama, T.4
  • 33
    • 0000286366 scopus 로고
    • Chemical and physical changes in red hake fillets during frozen storage
    • Owusu-Ansah, Y. J.; Hultin, H. O. Chemical and physical changes in red hake fillets during frozen storage. J. Food Sci. 1986, 51, 1402-1406.
    • (1986) J. Food Sci. , vol.51 , pp. 1402-1406
    • Owusu-Ansah, Y.J.1    Hultin, H.O.2
  • 34
    • 0022069871 scopus 로고
    • Solubilization of fish muscle proteins with buffers containing sodium dodecyl sulphate
    • Rehbein, H.; Karl, H. Solubilization of fish muscle proteins with buffers containing sodium dodecyl sulphate. Z. Lebensm. Unters. Forsch. 1985, 180, 373-378.
    • (1985) Z. Lebensm. Unters. Forsch. , vol.180 , pp. 373-378
    • Rehbein, H.1    Karl, H.2
  • 35
    • 0000665651 scopus 로고
    • Theories of protein denaturation during frozen storage of fish flesh
    • Shenouda, S. Y. K. Theories of protein denaturation during frozen storage of fish flesh. Adv. Food Res. 1980, 26, 275-311.
    • (1980) Adv. Food Res. , vol.26 , pp. 275-311
    • Shenouda, S.Y.K.1
  • 37
    • 0003103547 scopus 로고
    • Changes in proteins in frozen stored fish
    • Sikorski, Z. E., Sun Pan, B., Shahidi, F., Eds.; Chapman and Hall: New York
    • Sikorski, Z. E.; Kolakowska, A. Changes in proteins in frozen stored fish. In Seafood Proteins; Sikorski, Z. E., Sun Pan, B., Shahidi, F., Eds.; Chapman and Hall: New York, 1994; pp 99-231,
    • (1994) Seafood Proteins , pp. 99-231
    • Sikorski, Z.E.1    Kolakowska, A.2
  • 39
    • 0023487834 scopus 로고
    • Fluorescence energy transfer and membrane potential measurements monitor dynamic properties of cell membranes: A critical review
    • Szöllösi, J.; Damjanovich, S.; Mulhern, S. A.; Trón, L. Fluorescence energy transfer and membrane potential measurements monitor dynamic properties of cell membranes: a critical review. Prog. Biophys. Mol. Biol. 1987, 49, 65-87.
    • (1987) Prog. Biophys. Mol. Biol. , vol.49 , pp. 65-87
    • Szöllösi, J.1    Damjanovich, S.2    Mulhern, S.A.3    Trón, L.4
  • 42
    • 0017581208 scopus 로고
    • Changes of Raman scattering in the CH stretching region during thermally induced unfolding of ribonuclase
    • Verma, S. P.; Wallach, D. F. H. Changes of Raman scattering in the CH stretching region during thermally induced unfolding of ribonuclase. Biochem. Biophys. Res. Commun. 1977, 74, 473-479.
    • (1977) Biochem. Biophys. Res. Commun. , vol.74 , pp. 473-479
    • Verma, S.P.1    Wallach, D.F.H.2
  • 43
    • 0021095444 scopus 로고
    • Estimation of protein secondary structure from the laser Raman amide I spectrum
    • Williams, W. Estimation of protein secondary structure from the laser Raman amide I spectrum. J. Mol. Biol. 1983, 166, 581-603.
    • (1983) J. Mol. Biol. , vol.166 , pp. 581-603
    • Williams, W.1
  • 44
    • 0019882126 scopus 로고
    • Determination of the secondary structure of proteins from the amide I band of of the laser Raman spectrum
    • Williams, W.; Dunker, A. K. Determination of the secondary structure of proteins from the amide I band of of the laser Raman spectrum. J. Mol. Biol. 1981, 152, 783-813.
    • (1981) J. Mol. Biol. , vol.152 , pp. 783-813
    • Williams, W.1    Dunker, A.K.2
  • 45
    • 0015896965 scopus 로고
    • Laser Raman studies of conformational variations of poly-L-lysine
    • Yu, T. S.; Lippert, J. L.; Peticolas, W. L. Laser Raman studies of conformational variations of poly-L-lysine. Biopolymers. 1973, 12, 2161-2176.
    • (1973) Biopolymers , vol.12 , pp. 2161-2176
    • Yu, T.S.1    Lippert, J.L.2    Peticolas, W.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.