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Volumn 90, Issue 1-2, 2005, Pages 141-150

Physicochemical and biochemical changes during frozen storage of minced flesh of lizardfish (Saurida micropectoralis)

Author keywords

Denaturation; Dimethylamine; Formaldehyde; Frozen; Lizardfish TMAOase; Trimethylamine N oxide

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); DIMETHYLAMINE; FORMALDEHYDE; METHYLTRANSFERASE; OXYGEN; SODIUM CHLORIDE; TRIMETHYLAMINE OXIDE;

EID: 4644334737     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2004.03.038     Document Type: Article
Times cited : (77)

References (54)
  • 1
    • 85011222658 scopus 로고
    • A biological formation of FA in the muscle tissue of gadoid fish
    • Amano K., Yamada K. A biological formation of FA in the muscle tissue of gadoid fish. Nippon Suisan Gakkaishi. 30:1964;430-435
    • (1964) Nippon Suisan Gakkaishi , vol.30 , pp. 430-435
    • Amano, K.1    Yamada, K.2
  • 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. Journal of Food Science. 54:1989;814-818
    • (1989) Journal of Food Science , vol.54 , pp. 814-818
    • Ang, J.F.1    Hultin, H.O.2
  • 3
    • 0001340438 scopus 로고    scopus 로고
    • Freeze denaturation of carp myofibril compared with thermal denaturation
    • Azuma Y., Konno K. Freeze denaturation of carp myofibril compared with thermal denaturation. Fisheries Science. 64:1998;287-290
    • (1998) Fisheries Science , vol.64 , pp. 287-290
    • Azuma, Y.1    Konno, K.2
  • 4
    • 0006052142 scopus 로고    scopus 로고
    • A comparison of biochemical changes in cod (Gadus morhua) and haddock (Melanogrammus aeglefinus) during frozen storage
    • Baddii F., Howell N.K. A comparison of biochemical changes in cod (Gadus morhua) and haddock (Melanogrammus aeglefinus) during frozen storage. Journal of the Science of Food and Agriculture. 81:2001;1-11
    • (2001) Journal of the Science of Food and Agriculture , vol.81 , pp. 1-11
    • Baddii, F.1    Howell, N.K.2
  • 6
    • 0031462866 scopus 로고    scopus 로고
    • Physicochemical changes in Pacific whiting muscle proteins during iced storage
    • Benjakul S., Seymour T.S., Morrissey M.T., An H. Physicochemical changes in Pacific whiting muscle proteins during iced storage. Journal of Food Science. 62:1997;729-733
    • (1997) Journal of Food Science , vol.62 , pp. 729-733
    • Benjakul, S.1    Seymour, T.S.2    Morrissey, M.T.3    An, H.4
  • 7
    • 0142217339 scopus 로고    scopus 로고
    • Induced formation of dimethylamine and formaldehyde by lizardfish kidney trimethylamine-N-oxide demethylase
    • Benjakul S., Visessanguan W., Tanaka M. Induced formation of dimethylamine and formaldehyde by lizardfish kidney trimethylamine-. N -oxide demethylase Food Chemistry. 84:2004;297-305
    • (2004) Food Chemistry , vol.84 , pp. 297-305
    • Benjakul, S.1    Visessanguan, W.2    Tanaka, M.3
  • 8
    • 0037566099 scopus 로고    scopus 로고
    • Partial purification and characterization of trimethylamine-N-oxide demethylase from lizardfish kidney
    • Benjakul S., Visessanguan W., Tanaka M. Partial purification and characterization of trimethylamine-. N -oxide demethylase from lizardfish kidney Comparative Biochemistry Physiology Part B. 135:2003;359-371
    • (2003) Comparative Biochemistry Physiology Part B , vol.135 , pp. 359-371
    • Benjakul, S.1    Visessanguan, W.2    Tanaka, M.3
  • 9
    • 0042427804 scopus 로고    scopus 로고
    • Comparative study on physicochemical changes of muscle proteins from some tropical fish during frozen storage
    • Benjakul S., Visessanguan W., Thongkaew C., Tanaka M. Comparative study on physicochemical changes of muscle proteins from some tropical fish during frozen storage. Food Research International. 36:2003;787-795
    • (2003) Food Research International , vol.36 , pp. 787-795
    • Benjakul, S.1    Visessanguan, W.2    Thongkaew, C.3    Tanaka, M.4
  • 10
    • 84986430573 scopus 로고
    • Accelerated denaturation of myosin in frozen solution
    • Buttkus H. Accelerated denaturation of myosin in frozen solution. Journal of Food Science. 35:1970;558-562
    • (1970) Journal of Food Science , vol.35 , pp. 558-562
    • Buttkus, H.1
  • 11
    • 0014984073 scopus 로고
    • The sulfhydryl content of rabbit and trout myosins in relation to protein stability
    • Buttkus H. The sulfhydryl content of rabbit and trout myosins in relation to protein stability. Canadian Journal of Biochemistry. 49:1971;97-102
    • (1971) Canadian Journal of Biochemistry , vol.49 , pp. 97-102
    • Buttkus, H.1
  • 12
    • 84987339747 scopus 로고
    • On the nature of the chemical and physical bonds which contribute to some structural properties of protein foods: A hypothesis
    • Buttkus H. On the nature of the chemical and physical bonds which contribute to some structural properties of protein foods: A hypothesis. Journal of Food Science. 39:1974;484-489
    • (1974) Journal of Food Science , vol.39 , pp. 484-489
    • Buttkus, H.1
  • 13
    • 0031433220 scopus 로고    scopus 로고
    • Structural changes and Raman spectroscopic studies of cod myosin upon modification with formaldehyde or frozen storage
    • Careche M., Li-Chen E. Structural changes and Raman spectroscopic studies of cod myosin upon modification with formaldehyde or frozen storage. Journal of Food Science. 62:1997;717-723
    • (1997) Journal of Food Science , vol.62 , pp. 717-723
    • Careche, M.1    Li-Chen, E.2
  • 14
    • 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., Torrejon P., Tejada M. Importance of frozen storage temperature in the type of aggregation of myofibrillar proteins in cod (Gadus morhua) fillets. Journal of Agricultural and Food Chemistry. 46:1998;1539-1546
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 1539-1546
    • Careche, M.1    Del Mazo, M.L.2    Torrejon, P.3    Tejada, M.4
  • 15
    • 0001383217 scopus 로고
    • Comparison of changes in trimethylamine, dimethylamine and extractable protein in iced and frozen gadoid fillets
    • Castell C.H., Smith B., Dale J. Comparison of changes in trimethylamine, dimethylamine and extractable protein in iced and frozen gadoid fillets. Journal of the Fisheries Research Board of Canada. 30:1973;1246-1248
    • (1973) Journal of the Fisheries Research Board of Canada , vol.30 , pp. 1246-1248
    • Castell, C.H.1    Smith, B.2    Dale, J.3
  • 16
    • 0000093464 scopus 로고
    • An absorption apparatus for the micro determination of certain volatile substances. I. the micro-determination of ammonia
    • Conway E.J., Byrne A. An absorption apparatus for the micro determination of certain volatile substances. I. The micro-determination of ammonia. Biochemical Journal. 27:1936;419-429
    • (1936) Biochemical Journal , vol.27 , pp. 419-429
    • Conway, E.J.1    Byrne, A.2
  • 18
    • 0344299285 scopus 로고    scopus 로고
    • Characteristics of the salt-soluble fraction of hake (Merluccius merluccius) fillets stored at -20 and -30°C
    • Del Mazo M.L., Torrejon P., Careche M., Tejada M. Characteristics of the salt-soluble fraction of hake (Merluccius merluccius) fillets stored at -20 and -30°C. Journal of Agricultural and Food Chemistry. 47:1999;1372-1377
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , pp. 1372-1377
    • Del Mazo, M.L.1    Torrejon, P.2    Careche, M.3    Tejada, M.4
  • 20
    • 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 L.B. Textural deterioration of red hake and haddock muscle in frozen storage as related to chemical parameters and changes in the myofibrillar proteins. Journal of Food Science. 44:1979;661-667
    • (1979) Journal of Food Science , vol.44 , pp. 661-667
    • Gill, T.A.1    Keith, R.A.2    Smith, L.B.3
  • 22
    • 0006814424 scopus 로고
    • Delocalization of mitochondrial enzymes during freezing and thawing of skeletal muscle
    • O. R. Fennema (Ed.), Washington, DC: American Chemical Society
    • Hamm, R. (1979). Delocalization of mitochondrial enzymes during freezing and thawing of skeletal muscle. In O. R. Fennema (Ed.), Protein at Low Temperatures, Advances in Chemistry Series (Vol. 180, pp. 191). Washington, DC: American Chemical Society
    • (1979) Protein at Low Temperatures, Advances in Chemistry Series , vol.180 , pp. 191
    • Hamm, R.1
  • 23
    • 1842276056 scopus 로고
    • Effect of freezing and storage on the enzyme activities
    • Hatano S. Effect of freezing and storage on the enzyme activities. Refrigeration (Tokyo). 43:1968;14-20
    • (1968) Refrigeration (Tokyo) , vol.43 , pp. 14-20
    • Hatano, S.1
  • 24
    • 0001221912 scopus 로고
    • Contribution of hydrophobicity, net charge and sulfhydryl groups to thermal properties of ovalbumin
    • Hayagawa S., Nakai S. Contribution of hydrophobicity, net charge and sulfhydryl groups to thermal properties of ovalbumin. Canadian Institute of Food Science and Technology Journal. 18:1985;290-295
    • (1985) Canadian Institute of Food Science and Technology Journal , vol.18 , pp. 290-295
    • Hayagawa, S.1    Nakai, S.2
  • 25
    • 17544365196 scopus 로고    scopus 로고
    • Inhibition of formaldehyde production in frozen-stored minced blue whiting (Micromesistius poutassou) muscle by cryostabilizers: An approach from the glassy state theory
    • Herrera J.J., Pastoriza L., Sampedro G. Inhibition of formaldehyde production in frozen-stored minced blue whiting (Micromesistius poutassou) muscle by cryostabilizers: An approach from the glassy state theory. Journal of Agricultural and Food Chemistry. 48:2000;5256-5262
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 5256-5262
    • Herrera, J.J.1    Pastoriza, L.2    Sampedro, G.3
  • 26
    • 0000200547 scopus 로고    scopus 로고
    • Aggregation of myofibrillar proteins in hake, sardine and mixed minces during frozen storage
    • Huidobro A., Mohamed G.F., Tejada M. Aggregation of myofibrillar proteins in hake, sardine and mixed minces during frozen storage. Journal of Agricultural and Food Chemistry. 46:1998;2601-2608
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 2601-2608
    • Huidobro, A.1    Mohamed, G.F.2    Tejada, M.3
  • 27
    • 33845377898 scopus 로고
    • Changes in free amino acids and protein denaturation of fish muscle during frozen storage
    • Jiang S.T., Lee T.C. Changes in free amino acids and protein denaturation of fish muscle during frozen storage. Journal of Agricultural and Food Chemistry. 33:1985;839-844
    • (1985) Journal of Agricultural and Food Chemistry , vol.33 , pp. 839-844
    • Jiang, S.T.1    Lee, T.C.2
  • 28
    • 0000616237 scopus 로고
    • Effect of storage temperatures on the formation of disulfides and denaturation of milkfish actomyosin (Chanos chanos)
    • Jiang S.T., Hwang B.S., Chen C.S. Effect of storage temperatures on the formation of disulfides and denaturation of milkfish actomyosin (Chanos chanos). Journal of Food Science. 53:1988;1333-1335
    • (1988) Journal of Food Science , vol.53 , pp. 1333-1335
    • Jiang, S.T.1    Hwang, B.S.2    Chen, C.S.3
  • 29
    • 0001366044 scopus 로고
    • Denaturation and change in SH group of actomyosin from milkfish (Chanos chanos) during storage at -20°C
    • Jiang S.T., Hwang B.S., Chen C.S. Denaturation and change in SH group of actomyosin from milkfish (Chanos chanos) during storage at -20°C. Journal of Agricultural and Food Chemistry. 36:1988;433-437
    • (1988) Journal of Agricultural and Food Chemistry , vol.36 , pp. 433-437
    • Jiang, S.T.1    Hwang, B.S.2    Chen, C.S.3
  • 30
    • 84987277561 scopus 로고
    • Optimization of the freezing conditions on mackerel and amberfish for manufacturing minced fish
    • Jiang S.T., Ho M.L., lee T.C. Optimization of the freezing conditions on mackerel and amberfish for manufacturing minced fish. Journal of Food Science. 50:1985;727-732
    • (1985) Journal of Food Science , vol.50 , pp. 727-732
    • Jiang, S.T.1    Ho, M.L.2    Lee, T.C.3
  • 31
    • 84961006038 scopus 로고
    • The relationship between sulfhydryl groups and the activation of myosin adenosinetriphosphatase
    • Kielley W.W., Bradley L.B. The relationship between sulfhydryl groups and the activation of myosin adenosinetriphosphatase. The Journal of Biological Chemistry. 218:1956;653-659
    • (1956) The Journal of Biological Chemistry , vol.218 , pp. 653-659
    • Kielley, W.W.1    Bradley, L.B.2
  • 32
    • 0000002008 scopus 로고    scopus 로고
    • Occurrence and some properties of trimethylamine-N-oxide demethylase in myofibrillar fraction from walleye pollack muscle
    • Kimura M., Seki N., Kimura I. Occurrence and some properties of trimethylamine-. N -oxide demethylase in myofibrillar fraction from walleye pollack muscle Fisheries Science. 66:2000;725-729
    • (2000) Fisheries Science , vol.66 , pp. 725-729
    • Kimura, M.1    Seki, N.2    Kimura, I.3
  • 33
    • 0000157255 scopus 로고    scopus 로고
    • Purification and characterization of trimethylamine-N-oxide demethylase from walleye pollack muscle
    • Kimura M., Seki N., Kimura I. Purification and characterization of trimethylamine-. N -oxide demethylase from walleye pollack muscle Fisheries Science. 66:2000;967-973
    • (2000) Fisheries Science , vol.66 , pp. 967-973
    • Kimura, M.1    Seki, N.2    Kimura, I.3
  • 34
    • 84987316905 scopus 로고
    • Effect of chemical additives on toughening of fillets of frozen storage Alaska pollack (Theragra chacogramma)
    • Krueger D.J., Fennema O.R. Effect of chemical additives on toughening of fillets of frozen storage Alaska pollack (Theragra chacogramma). Journal of Food Science. 54:1989;1101-1106
    • (1989) Journal of Food Science , vol.54 , pp. 1101-1106
    • Krueger, D.J.1    Fennema, O.R.2
  • 36
    • 0001753731 scopus 로고
    • Enzymatic dimethylamine and formaldehyde production in minced American plaice and backbone flounder mixed with a red hake TMAOase active fraction
    • Lundstrom R.C., Correia F.F., Wilhelm K.A. Enzymatic dimethylamine and formaldehyde production in minced American plaice and backbone flounder mixed with a red hake TMAOase active fraction. Journal of Food Science. 47:1982;1305-1310
    • (1982) Journal of Food Science , vol.47 , pp. 1305-1310
    • Lundstrom, R.C.1    Correia, F.F.2    Wilhelm, K.A.3
  • 37
    • 84986533283 scopus 로고
    • Dimethylamine production in fresh red hake (Urophycis chuss): The effect of packaging material oxygen permeability and cellular damage
    • Lundstrom R.C., Correia F.F., Wilhelm K.A. Dimethylamine production in fresh red hake (Urophycis chuss): The effect of packaging material oxygen permeability and cellular damage. Journal of Food Biochemistry. 6:1983;229-241
    • (1983) Journal of Food Biochemistry , vol.6 , pp. 229-241
    • Lundstrom, R.C.1    Correia, F.F.2    Wilhelm, K.A.3
  • 38
    • 84985232093 scopus 로고
    • Effect of in situ formaldehyde production on solubility and crosslinking of proteins of minced red hake muscle during frozen storage
    • Owusu-Ansah Y.J., Hultin H.O. Effect of in situ formaldehyde production on solubility and crosslinking of proteins of minced red hake muscle during frozen storage. Journal of Food Biochemistry. 11:1987;17-39
    • (1987) Journal of Food Biochemistry , vol.11 , pp. 17-39
    • Owusu-Ansah, Y.J.1    Hultin, H.O.2
  • 39
    • 84986469612 scopus 로고
    • Some facts influencing the production of dimethylamine and formaldehyde in minced and intact red hake muscle
    • Parkin K.L., Hultin H.O. Some facts influencing the production of dimethylamine and formaldehyde in minced and intact red hake muscle. Journal of Food Processing and Preservation. 6:1982;73-97
    • (1982) Journal of Food Processing and Preservation , vol.6 , pp. 73-97
    • Parkin, K.L.1    Hultin, H.O.2
  • 40
    • 0020477208 scopus 로고
    • Fish muscle microsomes catalyze the conversion of trimethylamine oxide to dimethylamine and formaldehyde
    • Parkin K.L., Hultin H.O. Fish muscle microsomes catalyze the conversion of trimethylamine oxide to dimethylamine and formaldehyde. FEBS Letters. 139:1982;61-64
    • (1982) FEBS Letters , vol.139 , pp. 61-64
    • Parkin, K.L.1    Hultin, H.O.2
  • 41
    • 84986468612 scopus 로고
    • Distribution and some characteristics of trimethylamine-N-oxide (TMAO) demethylase activity of red hake muscle
    • Phillipy B.Q., Hultin H.O. Distribution and some characteristics of trimethylamine-. N -oxide (TMAO) demethylase activity of red hake muscle Journal of Food Biochemistry. 17:1993;235-250
    • (1993) Journal of Food Biochemistry , vol.17 , pp. 235-250
    • Phillipy, B.Q.1    Hultin, H.O.2
  • 42
    • 16744366516 scopus 로고    scopus 로고
    • Fish myosin aggregation as affected by freezing and initial physical state
    • Ramirez J.A., Martin-Polo M.O., Bandman E. Fish myosin aggregation as affected by freezing and initial physical state. Journal of Food Science. 65:2000;556-560
    • (2000) Journal of Food Science , vol.65 , pp. 556-560
    • Ramirez, J.A.1    Martin-Polo, M.O.2    Bandman, E.3
  • 43
    • 0021726053 scopus 로고
    • TMAOase activity in tissues of fish species from the Northeast Atlantic
    • Rehbein H., Schreiber W. TMAOase activity in tissues of fish species from the Northeast Atlantic. Comparative Biochemistry Physiology Part B. 79:1984;447-452
    • (1984) Comparative Biochemistry Physiology Part B , vol.79 , pp. 447-452
    • Rehbein, H.1    Schreiber, W.2
  • 44
    • 0000665651 scopus 로고
    • Theories of protein denaturation during frozen storage of fish flesh
    • C.O. Chichester. New York: Academic Press
    • Shenouda S.Y.K. Theories of protein denaturation during frozen storage of fish flesh. Chichester C.O. Advance in Food Research. 1980;275 Academic Press, New York
    • (1980) Advance in Food Research , pp. 275
    • Shenouda, S.Y.K.1
  • 46
    • 0001181571 scopus 로고    scopus 로고
    • Effect of frozen storage on the quality of whole fish and fillets of horse mackerel (Trachurus trachurus) and Mediterranean hake (Merluccius mediteraneus)
    • Simeonidou S., Govaris A., Vareltzis K. Effect of frozen storage on the quality of whole fish and fillets of horse mackerel (Trachurus trachurus) and Mediterranean hake (Merluccius mediteraneus). Zeitschrift fur Lebensmittel-Untersuchung und-Forschung. 204:1997;405-410
    • (1997) Zeitschrift fur Lebensmittel-Untersuchung Und-Forschung , vol.204 , pp. 405-410
    • Simeonidou, S.1    Govaris, A.2    Vareltzis, K.3
  • 47
    • 0001048082 scopus 로고    scopus 로고
    • Effect of cryoprotectants and reducing reagent on the stability of actomyosin during ice storage
    • Sompongse E., Itoh Y., Obataka A. Effect of cryoprotectants and reducing reagent on the stability of actomyosin during ice storage. Fisheries Science. 62:1996;110-113
    • (1996) Fisheries Science , vol.62 , pp. 110-113
    • Sompongse, E.1    Itoh, Y.2    Obataka, A.3
  • 50
    • 0034775207 scopus 로고    scopus 로고
    • Structural changes in natural actomyosin and surimi from ling cod (Ophiodon elongates) during frozen storage in the absence or presence of cryoprotectants
    • Sultanbawa Y., Li-Chan E.C.Y. Structural changes in natural actomyosin and surimi from ling cod (Ophiodon elongates) during frozen storage in the absence or presence of cryoprotectants. Journal of Agricultural and Food Chemistry. 49:2001;4716-4725
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , pp. 4716-4725
    • Sultanbawa, Y.1    Li-Chan, E.C.Y.2
  • 51
    • 0038312407 scopus 로고
    • Freezing denaturation of fish proteins
    • Suzuki T. Freezing denaturation of fish proteins. Refrigeration (Tokyo). 42:1967;46-51
    • (1967) Refrigeration (Tokyo) , vol.42 , pp. 46-51
    • Suzuki, T.1
  • 52
  • 54
    • 0012905963 scopus 로고
    • Changes in chemical and physical properties of lizardfish meat during iced and frozen storage
    • Yasui A., Lim P.Y. Changes in chemical and physical properties of lizardfish meat during iced and frozen storage. Nippon Shokuhin Kyogo Gakkaishi. 34:1987;54-60
    • (1987) Nippon Shokuhin Kyogo Gakkaishi , vol.34 , pp. 54-60
    • Yasui, A.1    Lim, P.Y.2


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