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Volumn 81, Issue 2, 2007, Pages 492-499

Rheological properties of selected fish paste at selected temperature pertaining to shaping of surimi-based products

Author keywords

Electrophoresis; Fish meat paste; Interval thixotropy analysis; Storage modulus; Temperature sweep analysis; Thermal gel shaping; Viscoelasticity

Indexed keywords

ELECTROPHORESIS; GELS; MEATS; RHEOLOGY; THERMAL EFFECTS; VISCOELASTICITY;

EID: 33846872789     PISSN: 02608774     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jfoodeng.2006.11.029     Document Type: Article
Times cited : (30)

References (36)
  • 2
    • 0027847854 scopus 로고
    • Towards a phenomenological definition of the term 'gel'
    • Almdal K., Dyre J., Hvidt S., and Kramer O. Towards a phenomenological definition of the term 'gel'. Polymer Gels Networks 1 (1992) 15-17
    • (1992) Polymer Gels Networks , vol.1 , pp. 15-17
    • Almdal, K.1    Dyre, J.2    Hvidt, S.3    Kramer, O.4
  • 3
    • 21144480080 scopus 로고
    • Comparison of reactivity of transglutaminase to various fish actomyosins
    • Araki H., and Seki N. Comparison of reactivity of transglutaminase to various fish actomyosins. Nippon Suisan Gakkaishi 59 (1993) 711-716
    • (1993) Nippon Suisan Gakkaishi , vol.59 , pp. 711-716
    • Araki, H.1    Seki, N.2
  • 5
    • 0000724738 scopus 로고
    • The relative stabilities of the skeletal muscle myosin of some animals
    • Connell J.J. The relative stabilities of the skeletal muscle myosin of some animals. Biochemical Journal 80 (1961) 503-509
    • (1961) Biochemical Journal , vol.80 , pp. 503-509
    • Connell, J.J.1
  • 6
    • 21844508379 scopus 로고
    • Rheological parameters as predictor of protein functionality: a model study using myofibrils of different fiber-type composition
    • Egelandsdal B., Martinsen B., and Autio K. Rheological parameters as predictor of protein functionality: a model study using myofibrils of different fiber-type composition. Meat Science 39 (1995) 97-111
    • (1995) Meat Science , vol.39 , pp. 97-111
    • Egelandsdal, B.1    Martinsen, B.2    Autio, K.3
  • 7
    • 0038573664 scopus 로고    scopus 로고
    • Thermal effects on fast skeletal myosins from Alaska pollock, white croaker, and rabbit in relation to gel formation
    • Fukushima H., Satoh Y., Nakaya M., Ishizaki S., and Watabe S. Thermal effects on fast skeletal myosins from Alaska pollock, white croaker, and rabbit in relation to gel formation. Journal of Food Science 68 (2003) 1573-1577
    • (2003) Journal of Food Science , vol.68 , pp. 1573-1577
    • Fukushima, H.1    Satoh, Y.2    Nakaya, M.3    Ishizaki, S.4    Watabe, S.5
  • 8
    • 28444467468 scopus 로고    scopus 로고
    • Rheological properties of fast skeletal myosin rod and light meromyosin from walleye pollack and white croaker: contribution of myosin fragments to thermal gel formation
    • Fukushima H., Satoh Y., Yoon S.H., Togashi M., Nakaya M., and Watabe S. Rheological properties of fast skeletal myosin rod and light meromyosin from walleye pollack and white croaker: contribution of myosin fragments to thermal gel formation. Journal of Agricultural and Food Chemistry 53 (2005) 9193-9198
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 9193-9198
    • Fukushima, H.1    Satoh, Y.2    Yoon, S.H.3    Togashi, M.4    Nakaya, M.5    Watabe, S.6
  • 9
    • 0038691746 scopus 로고    scopus 로고
    • Differences in polymer formation through disulfide bonding of recombinant light meromyosin between white croaker and walleye pollack and their possible relation to species-specific differences in thermal unfolding
    • Fukushima H., Yoon S.H., and Watabe S. Differences in polymer formation through disulfide bonding of recombinant light meromyosin between white croaker and walleye pollack and their possible relation to species-specific differences in thermal unfolding. Journal of Agricultural and Food Chemistry 51 (2003) 4089-4095
    • (2003) Journal of Agricultural and Food Chemistry , vol.51 , pp. 4089-4095
    • Fukushima, H.1    Yoon, S.H.2    Watabe, S.3
  • 10
    • 0008731195 scopus 로고
    • Rheology: a tool for understanding thermally induced protein gelation
    • Interactions of food proteins. Parris N., and Barford R. (Eds), American Chemical Society, Washington, DC
    • Hamann D.D. Rheology: a tool for understanding thermally induced protein gelation. In: Parris N., and Barford R. (Eds). Interactions of food proteins. ACS symposium series vol. 454 (1991), American Chemical Society, Washington, DC 212-227
    • (1991) ACS symposium series , vol.454 , pp. 212-227
    • Hamann, D.D.1
  • 12
    • 0034451721 scopus 로고    scopus 로고
    • Determination of primary structure of amberjack myosin heavy chain and its relationship with structural stability of various fish myosin rods
    • Kawabata R., Kanzawa N., Ogawa M., and Tsuchiya T. Determination of primary structure of amberjack myosin heavy chain and its relationship with structural stability of various fish myosin rods. Fish Physiology and Biochemistry 23 (2000) 283-294
    • (2000) Fish Physiology and Biochemistry , vol.23 , pp. 283-294
    • Kawabata, R.1    Kanzawa, N.2    Ogawa, M.3    Tsuchiya, T.4
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0002834962 scopus 로고
    • Surimi processing technology
    • Lee C.M. Surimi processing technology. Food Technology 38 (1984) 69-80
    • (1984) Food Technology , vol.38 , pp. 69-80
    • Lee, C.M.1
  • 16
    • 85008120416 scopus 로고
    • Gel forming ability and cross-linking ability of myosin heavy chain in salted meat paste from threadfin bream
    • Lee N., Seki N., Kato N., Nakagawa N., Terui S., and Arai K. Gel forming ability and cross-linking ability of myosin heavy chain in salted meat paste from threadfin bream. Nippon Suisan Gakkaishi 56 (1990) 329-336
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 329-336
    • Lee, N.1    Seki, N.2    Kato, N.3    Nakagawa, N.4    Terui, S.5    Arai, K.6
  • 17
    • 84986736089 scopus 로고
    • Relationship between functional and physicochemical properties of muscle proteins
    • Li-Chan E., Nakai S., and Wood D. Relationship between functional and physicochemical properties of muscle proteins. Journal of Food Science 50 (1985) 1034-1040
    • (1985) Journal of Food Science , vol.50 , pp. 1034-1040
    • Li-Chan, E.1    Nakai, S.2    Wood, D.3
  • 18
    • 84985204868 scopus 로고
    • Thermally induced gelation of selected comminuted muscle systems: rheological changes during processing, final strengths and microstructure
    • Montejano J.G., Hamann D.D., and Lanier T.C. Thermally induced gelation of selected comminuted muscle systems: rheological changes during processing, final strengths and microstructure. Journal of Food Science 49 (1984) 1496-1505
    • (1984) Journal of Food Science , vol.49 , pp. 1496-1505
    • Montejano, J.G.1    Hamann, D.D.2    Lanier, T.C.3
  • 19
    • 2442608766 scopus 로고
    • The Iwanami Shoten, Co., Ltd., Tokyo
    • Nakagawa T. Rheology. 2nd ed. (1978), The Iwanami Shoten, Co., Ltd., Tokyo
    • (1978) Rheology. 2nd ed.
    • Nakagawa, T.1
  • 20
    • 85008094000 scopus 로고
    • Temperature-dependent changes in gel strength and myosin heavy-chain of salt-ground meat from walleye pollack during setting
    • Numakura T., Kimura I., Toyoda K., and Fujita T. Temperature-dependent changes in gel strength and myosin heavy-chain of salt-ground meat from walleye pollack during setting. Nippon Suisan Gakkaishi 56 (1990) 2035-2043
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 2035-2043
    • Numakura, T.1    Kimura, I.2    Toyoda, K.3    Fujita, T.4
  • 23
    • 0002568649 scopus 로고
    • History of surimi technology in Japan
    • Marcel Dekker, Inc., New York
    • Okada M. History of surimi technology in Japan. Surimi technology (1992), Marcel Dekker, Inc., New York 3-21
    • (1992) Surimi technology , pp. 3-21
    • Okada, M.1
  • 24
    • 84971620957 scopus 로고
    • Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation
    • Sano T., Noguchi S.F., Tsuchiya T., and Matsumoto J.J. Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation. Journal of Food Science 53 (1988) 924-928
    • (1988) Journal of Food Science , vol.53 , pp. 924-928
    • Sano, T.1    Noguchi, S.F.2    Tsuchiya, T.3    Matsumoto, J.J.4
  • 25
    • 85008134027 scopus 로고
    • Transglutaminase activity in Alaska pollack muscle and surimi, and its reaction with myosin B
    • Seki N., Uno H., Lee N., Kimura I., Toyoda K., Fujita T., et al. Transglutaminase activity in Alaska pollack muscle and surimi, and its reaction with myosin B. Nippon Suisan Gakkaishi 56 (1990) 125-132
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 125-132
    • Seki, N.1    Uno, H.2    Lee, N.3    Kimura, I.4    Toyoda, K.5    Fujita, T.6
  • 26
    • 85008099502 scopus 로고
    • Properties of kamaboko gels prepared by using a new heating apparatus
    • Shiba M. Properties of kamaboko gels prepared by using a new heating apparatus. Nippon Suisan Gakkaishi 58 (1992) 895-901
    • (1992) Nippon Suisan Gakkaishi , vol.58 , pp. 895-901
    • Shiba, M.1
  • 27
    • 33846882431 scopus 로고
    • Development of continuous manufacturing apparatus for kamaboko gel by applying joule heat, and the resultant quality of kamaboko gel
    • Shiba M. Development of continuous manufacturing apparatus for kamaboko gel by applying joule heat, and the resultant quality of kamaboko gel. Nippon Suisan Gakkaishi 59 (1993) 795-800
    • (1993) Nippon Suisan Gakkaishi , vol.59 , pp. 795-800
    • Shiba, M.1
  • 28
    • 85007897180 scopus 로고
    • Rheological properties and structure of kamaboko. Influence of suwari upon viscoelastic properties and structures of fish muscle paste and kamaboko
    • Takagi I. Rheological properties and structure of kamaboko. Influence of suwari upon viscoelastic properties and structures of fish muscle paste and kamaboko. Bulletin of the Japanese Society of Scientific Fisheries 39 (1973) 299-305
    • (1973) Bulletin of the Japanese Society of Scientific Fisheries , vol.39 , pp. 299-305
    • Takagi, I.1
  • 29
    • 0037077363 scopus 로고    scopus 로고
    • Differential scanning calorimetry and circular dichroism spectrometry of walleye pollack myosin and light meromyosin
    • Togashi M., Kakinuma M., Nakaya M., Ooi T., and Watabe S. Differential scanning calorimetry and circular dichroism spectrometry of walleye pollack myosin and light meromyosin. Journal of Agricultural and Food Chemistry 50 (2002) 4803-4811
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , pp. 4803-4811
    • Togashi, M.1    Kakinuma, M.2    Nakaya, M.3    Ooi, T.4    Watabe, S.5
  • 30
    • 0039490373 scopus 로고    scopus 로고
    • Rheological methods for assessment of food freshness and stability
    • Freshness and shelf life of foods. Cadwallader K.R., and Weenen H. (Eds), American Chemical Society, Washington, DC
    • Truong V.D., and Daubert C.R. Rheological methods for assessment of food freshness and stability. In: Cadwallader K.R., and Weenen H. (Eds). Freshness and shelf life of foods. ACS symposium series vol. 836 (2003), American Chemical Society, Washington, DC 248-268
    • (2003) ACS symposium series , vol.836 , pp. 248-268
    • Truong, V.D.1    Daubert, C.R.2
  • 31
    • 0036692572 scopus 로고    scopus 로고
    • Total activity of transglutaminase at various temperatures in several fish meats
    • Tsukamasa Y., Miyake Y., Ando M., and Makinodan Y. Total activity of transglutaminase at various temperatures in several fish meats. Fisheries Science 68 (2002) 929-933
    • (2002) Fisheries Science , vol.68 , pp. 929-933
    • Tsukamasa, Y.1    Miyake, Y.2    Ando, M.3    Makinodan, Y.4
  • 32
    • 85008070668 scopus 로고
    • Setting property of sardine and pacific mackerel meat
    • Tsukamasa Y., and Shimizu Y. Setting property of sardine and pacific mackerel meat. Nippon Suisan Gakkaishi 56 (1990) 1105-1112
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 1105-1112
    • Tsukamasa, Y.1    Shimizu, Y.2
  • 33
    • 0000305306 scopus 로고
    • Factors affecting the transglutaminase-associated setting phenomenon in fish meat sol
    • Tsukamasa Y., and Shimizu Y. Factors affecting the transglutaminase-associated setting phenomenon in fish meat sol. Nippon Suisan Gakkaishi 57 (1991) 535-540
    • (1991) Nippon Suisan Gakkaishi , vol.57 , pp. 535-540
    • Tsukamasa, Y.1    Shimizu, Y.2
  • 34
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber K., and Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. Journal of Biological Chemistry 244 (1969) 4404-4412
    • (1969) Journal of Biological Chemistry , vol.244 , pp. 4404-4412
    • Weber, K.1    Osborn, M.2
  • 35
    • 66349092322 scopus 로고    scopus 로고
    • Fish cake
    • Koseisha Koseikaku, Co., Ltd., Tokyo
    • Yamazawa M., Seki N., and Fukuda Y. Fish cake. Kamaboko (2003), Koseisha Koseikaku, Co., Ltd., Tokyo 212
    • (2003) Kamaboko , pp. 212
    • Yamazawa, M.1    Seki, N.2    Fukuda, Y.3
  • 36
    • 0041386023 scopus 로고    scopus 로고
    • Thermal denaturation and aggregation of threadfin bream actomyosin
    • Yongsawatdigul J., and Park J.W. Thermal denaturation and aggregation of threadfin bream actomyosin. Food Chemistry 83 (2003) 409-416
    • (2003) Food Chemistry , vol.83 , pp. 409-416
    • Yongsawatdigul, J.1    Park, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.