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Volumn 19, Issue 2, 2005, Pages 197-207

Effect of frozen storage on chemical and gel-forming properties of fish commonly used for surimi production in Thailand

Author keywords

Denaturation; Formaldehyde; Frozen storage; Gel forming ability; Surimi

Indexed keywords

CHLORINE COMPOUNDS; DENATURATION; FISH; POTASSIUM COMPOUNDS; PROTEINS; SOLUBILITY;

EID: 8644278895     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2004.05.004     Document Type: Article
Times cited : (165)

References (43)
  • 1
    • 0034041511 scopus 로고    scopus 로고
    • Physicochemical and enzymatic changes of cod muscle proteins subjected to different freeze-thaw cycles
    • Benjakul S., Bauer F. Physicochemical and enzymatic changes of cod muscle proteins subjected to different freeze-thaw cycles. Journal of the Science of Food Agriculture. 80:2000;1143-1150
    • (2000) Journal of the Science of Food Agriculture , vol.80 , pp. 1143-1150
    • Benjakul, S.1    Bauer, F.2
  • 2
    • 0035179693 scopus 로고    scopus 로고
    • Biochemical and physicochemical changes in catfish (Silurus glanis Linne) muscle as influenced by different freeze-thaw cylces
    • Benjakul S., Bauer F. Biochemical and physicochemical changes in catfish (Silurus glanis Linne) muscle as influenced by different freeze-thaw cylces. Food Chemistry. 72:2001;207-217
    • (2001) Food Chemistry , vol.72 , pp. 207-217
    • Benjakul, S.1    Bauer, F.2
  • 3
    • 0031462866 scopus 로고    scopus 로고
    • Physicochemical changes in Pacific whiting muscle proteins during iced storage
    • Benjakul S., Seymour T.A., 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.A.2    Morrissey, M.T.3    An, H.4
  • 4
    • 0035665007 scopus 로고    scopus 로고
    • Differences in gelation characteristics of natural actomyosin from two species of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus
    • Benjakul S., Visessanguan W., Ishizaki S., Tanaka M. Differences in gelation characteristics of natural actomyosin from two species of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus. Journal of Food Science. 66:2000;1311-1318
    • (2000) Journal of Food Science , vol.66 , pp. 1311-1318
    • Benjakul, S.1    Visessanguan, W.2    Ishizaki, S.3    Tanaka, M.4
  • 6
    • 0035457403 scopus 로고    scopus 로고
    • Porcine plasma proteins as gel enhancer in bigeye snapper (Priacanthus tayenus) surimi
    • Benjakul S., Visessanguan W., Srivilai C. Porcine plasma proteins as gel enhancer in bigeye snapper (Priacanthus tayenus) surimi. Journal of Food Biochemistry. 25:2001;285-305
    • (2001) Journal of Food Biochemistry , vol.25 , pp. 285-305
    • Benjakul, S.1    Visessanguan, W.2    Srivilai, C.3
  • 7
    • 0037566099 scopus 로고    scopus 로고
    • Partial purification and characterization of trimethyl-N-oxide demethylase from lizardfish kidney
    • Benjakul S., Visessangaun W., Tanaka M. Partial purification and characterization of trimethyl-N-oxide demethylase from lizardfish kidney. Comparative Biochemistry and Physiology, Part B. 135:2003;359-371
    • (2003) Comparative Biochemistry and Physiology, Part B , vol.135 , pp. 359-371
    • Benjakul, S.1    Visessangaun, W.2    Tanaka, M.3
  • 8
    • 0042427804 scopus 로고    scopus 로고
    • Comparative study on physicochemical changes of muscle proteins from some tropical fish during frozen storage
    • Benjakul S., Visessanguan W., Thongkeaw 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    Thongkeaw, C.3    Tanaka, M.4
  • 9
    • 0037388169 scopus 로고    scopus 로고
    • Changes in physico-chemical properties and gel-forming ability of lizardfish (Saurida tumbil) during post-mortem storage in ice
    • Benjakul S., Visessanguan W., Tueksuban J. Changes in physico-chemical properties and gel-forming ability of lizardfish (Saurida tumbil) during post-mortem storage in ice. Food Chemistry. 80:2003;535-544
    • (2003) Food Chemistry , vol.80 , pp. 535-544
    • Benjakul, S.1    Visessanguan, W.2    Tueksuban, J.3
  • 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
    • 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
  • 12
    • 84986808912 scopus 로고
    • The role of formaldehyde as a protein crosslinking agent acting during the frozen storage of cod
    • Connell J.J. The role of formaldehyde as a protein crosslinking agent acting during the frozen storage of cod. Journal of the Science of Food and Agriculture. 26:1975;1925-1929
    • (1975) Journal of the Science of Food and Agriculture , vol.26 , pp. 1925-1929
    • Connell, J.J.1
  • 14
    • 0000616237 scopus 로고
    • Effect of storage temperature on the formation of disulfide and denaturation on milkfish actomyosin (Chanos chanos)
    • Jiang S.T., Hwang D.C., Chen C.S. Effect of storage temperature on the formation of disulfide and denaturation on 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, D.C.2    Chen, C.S.3
  • 15
    • 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
  • 19
    • 84986517574 scopus 로고
    • Protein insolubilization in frozen Greenland halibut (Reinhardtius hippoglossoides)
    • Lim H.K., Haard N.F. Protein insolubilization in frozen Greenland halibut (Reinhardtius hippoglossoides). Journal of Food Biochemistry. 8:1984;163-187
    • (1984) Journal of Food Biochemistry , vol.8 , pp. 163-187
    • Lim, H.K.1    Haard, N.F.2
  • 20
    • 84986533283 scopus 로고
    • Dimethylamine production in fresh red hake (Urophycis chuss): The effect of packaging material on 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 on oxygen permeability and cellular damage. Journal of Food Biochemistry. 6:1982;229-241
    • (1982) Journal of Food Biochemistry , vol.6 , pp. 229-241
    • Lundstrom, R.C.1    Correia, F.F.2    Wilhelm, K.A.3
  • 21
    • 84986456525 scopus 로고
    • The strength of gels prepared from washed and unwashed minces of hoki (Macruronus novaezelandiae) stored in ice
    • MacDonald G.A., Lelievre J., Wilson N.D.C. The strength of gels prepared from washed and unwashed minces of hoki (Macruronus novaezelandiae) stored in ice. Journal of Food Science. 55:1990;976-980
    • (1990) Journal of Food Science , vol.55 , pp. 976-980
    • MacDonald, G.A.1    Lelievre, J.2    Wilson, N.D.C.3
  • 22
    • 84987285039 scopus 로고
    • Effect of frozen storage on the gel-forming properties of hoki (Macruronus novaezelandiae)
    • MacDonald G.A., Lelievre J., Wilson N.D.C. Effect of frozen storage on the gel-forming properties of hoki (Macruronus novaezelandiae). Journal of Food Science. 57:1992;69-73
    • (1992) Journal of Food Science , vol.57 , pp. 69-73
    • MacDonald, G.A.1    Lelievre, J.2    Wilson, N.D.C.3
  • 23
    • 0002120573 scopus 로고
    • Chemical deterioration of muscle proteins during frozen storage
    • Matsumoto J.J. Chemical deterioration of muscle proteins during frozen storage. American Chemistry Society Symposium Series. 123:1980;95-124
    • (1980) American Chemistry Society Symposium Series , vol.123 , pp. 95-124
    • Matsumoto, J.J.1
  • 24
    • 0003374658 scopus 로고
    • ATPase and lactate dehydrogenase activities in frozen stored fish muscle as indices of cold storage deterioration
    • Nambudiri D.D., Gopakumar K. ATPase and lactate dehydrogenase activities in frozen stored fish muscle as indices of cold storage deterioration. Journal of Food Science. 57:1992;72-76
    • (1992) Journal of Food Science , vol.57 , pp. 72-76
    • Nambudiri, D.D.1    Gopakumar, K.2
  • 25
    • 77049138167 scopus 로고
    • The colorimetric estimation of formaldehyde by means of the Hantzsch reaction
    • Nash T. The colorimetric estimation of formaldehyde by means of the Hantzsch reaction. Biochemical Journal. 55:1953;416-421
    • (1953) Biochemical Journal , vol.55 , pp. 416-421
    • Nash, T.1
  • 26
    • 0002430694 scopus 로고    scopus 로고
    • Manufacturing of surimi from light muscle fish
    • J.W. Park. New York: Marcel Dekker
    • Park J.W., Morrissey M.T. Manufacturing of surimi from light muscle fish. Park J.W. Surimi and surimi seafood. 2000;23-58 Marcel Dekker, New York
    • (2000) Surimi and Surimi Seafood , pp. 23-58
    • Park, J.W.1    Morrissey, M.T.2
  • 27
    • 84986469612 scopus 로고
    • Some factors influencing the production of dimethylamine and formaldehyde in minced and intact red hake muscle
    • Parking K.L., Hultin H.O. Some factors 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
    • Parking, K.L.1    Hultin, H.O.2
  • 29
    • 84986468612 scopus 로고
    • Distribution and some characteristics of trimethylamine N-oxide demethylase activity of red hake muscle
    • Phillippy B.Q., Hultin H.O. Distribution and some characteristics of trimethylamine N-oxide demethylase activity of red hake muscle. Journal of Food Biochemistry. 17:1993;235-250
    • (1993) Journal of Food Biochemistry , vol.17 , pp. 235-250
    • Phillippy, B.Q.1    Hultin, H.O.2
  • 31
    • 0000451299 scopus 로고
    • The biuret reaction in the determination of serum protein. I. a study of the condition necessary for the production of the stable color which bears a quantitative relationship to the protein concentration
    • Robinson H.W., Hodgen C.G. The biuret reaction in the determination of serum protein. I. A study of the condition necessary for the production of the stable color which bears a quantitative relationship to the protein concentration. Journal of the Biological Chemistry. 135:1940;707-725
    • (1940) Journal of the Biological Chemistry , vol.135 , pp. 707-725
    • Robinson, H.W.1    Hodgen, C.G.2
  • 32
    • 0032821131 scopus 로고    scopus 로고
    • Electron spin resonance (ESR) study on free-radical transfer in fish lipid-protein interactions
    • Saeed S., Fawthrop S.A., Howell N.K. Electron spin resonance (ESR) study on free-radical transfer in fish lipid-protein interactions. Journal of the Science of Food and Agriculture. 79:1999;1809-1816
    • (1999) Journal of the Science of Food and Agriculture , vol.79 , pp. 1809-1816
    • Saeed, S.1    Fawthrop, S.A.2    Howell, N.K.3
  • 33
    • 0036218461 scopus 로고    scopus 로고
    • Effect of lipid oxidation and frozen storage on muscle proteins of Atlantic mackerel (Scomber scombrus)
    • Saeed S., Howell N.K. Effect of lipid oxidation and frozen storage on muscle proteins of Atlantic mackerel (Scomber scombrus). Journal of the Science of Food and Agriculture. 82:2002;579-586
    • (2002) Journal of the Science of Food and Agriculture , vol.82 , pp. 579-586
    • Saeed, S.1    Howell, N.K.2
  • 35
    • 84987368757 scopus 로고
    • Effect of ionic strength on dynamic viscoelastic behavior of myosin during thermal gelation
    • Sano T., Noguchi S.F., Matsumoto J.J., Tsuchiya T. Effect of ionic strength on dynamic viscoelastic behavior of myosin during thermal gelation. Journal of Food Science. 55:1990;51-54
    • (1990) Journal of Food Science , vol.55 , pp. 51-54
    • Sano, T.1    Noguchi, S.F.2    Matsumoto, J.J.3    Tsuchiya, T.4
  • 36
    • 84987301335 scopus 로고
    • Effect of freezing and frozen storage of Alaska pollock on the chemical and gel-forming properties of surimi
    • Scott D.N., Porter R.W., Kudo G., Miller R., Koury B. Effect of freezing and frozen storage of Alaska pollock on the chemical and gel-forming properties of surimi. Journal of Food Science. 53:1988;353-359
    • (1988) Journal of Food Science , vol.53 , pp. 353-359
    • Scott, D.N.1    Porter, R.W.2    Kudo, G.3    Miller, R.4    Koury, B.5
  • 42
    • 0000016866 scopus 로고    scopus 로고
    • Protein denaturation and functionality losses
    • M.C. Erickson, & Y.C. Huang. New York: Chapman & Hall
    • Xiong Y.L. Protein denaturation and functionality losses. Erickson M.C., Huang Y.C. Quality in frozen food. 1997;111-140 Chapman & Hall, New York
    • (1997) Quality in Frozen Food , pp. 111-140
    • Xiong, Y.L.1
  • 43
    • 85011222637 scopus 로고
    • Studies on the biological formation of formaldehyde and dimethylamine in fish and shellfish. VII. Effect of methylene blue on the enzymatic formation of formaldehyde and dimethylamine from trimethylamine oxide
    • Yamada K., Amano K. Studies on the biological formation of formaldehyde and dimethylamine in fish and shellfish. VII. Effect of methylene blue on the enzymatic formation of formaldehyde and dimethylamine from trimethylamine oxide. Bulletin of the Japanese Society of Scientific Fisheries. 31:1965;1030-1037
    • (1965) Bulletin of the Japanese Society of Scientific Fisheries , vol.31 , pp. 1030-1037
    • Yamada, K.1    Amano, K.2


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