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Volumn 79, Issue 4, 2013, Pages 715-724

Thermal gelation properties of white croaker, walleye pollack and deepsea bonefish surimi after suwari treatment at various temperatures

Author keywords

Cross linking; Deepsea bonefish; Fish meat; Myosin; Suwari; Thermal gelation

Indexed keywords

ALBULIDAE; GENYONEMUS LINEATUS; POLLACHIUS POLLACHIUS; STIZOSTEDION VITREUM;

EID: 84880635040     PISSN: 09199268     EISSN: 14442906     Source Type: Journal    
DOI: 10.1007/s12562-013-0640-7     Document Type: Article
Times cited : (25)

References (44)
  • 1
    • 85008110152 scopus 로고
    • Studies on muscle of aquatic animals-IV. On the so-called setting and modori phenomenon (in Japanese)
    • Simizu W (1944) Studies on muscle of aquatic animals-IV. On the so-called setting and modori phenomenon (in Japanese). Nippon Suisan Gakkaishi 12: 165-172.
    • (1944) Nippon Suisan Gakkaishi , vol.12 , pp. 165-172
    • Simizu, W.1
  • 4
    • 0005184257 scopus 로고
    • Kamaboko formation of mackerel and red sea bream myosins
    • Iwata K, Kanna K, Okada M (1977) Kamaboko formation of mackerel and red sea bream myosins. Nippon Suisan Gakkaishi 43: 237.
    • (1977) Nippon Suisan Gakkaishi , vol.43 , pp. 237
    • Iwata, K.1    Kanna, K.2    Okada, M.3
  • 5
    • 85008134027 scopus 로고
    • Transglutaminase activity in Alaska pollack muscle and surimi, and its reaction with myosin B (in Japanese with English abstract)
    • Seki N, Uno H, Lee NH, Kimura I, Toyoda K, Fujita T, Arai K (1990) Transglutaminase activity in Alaska pollack muscle and surimi, and its reaction with myosin B (in Japanese with English abstract). Nippon Suisan Gakkaishi 56: 125-132.
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 125-132
    • Seki, N.1    Uno, H.2    Lee, N.H.3    Kimura, I.4    Toyoda, K.5    Fujita, T.6    Arai, K.7
  • 6
    • 21344474722 scopus 로고    scopus 로고
    • The effect of setting temperature on the relationship between ε-(γ-glutamyl)lysine crosslink content and breaking strength in salt-ground meat of sardine and Alaska pollack (in Japanese with English abstract)
    • Imai C, Tsukamasa Y, Sugiyama M, Minegishi Y, Shimizu Y (1996) The effect of setting temperature on the relationship between ε-(γ-glutamyl)lysine crosslink content and breaking strength in salt-ground meat of sardine and Alaska pollack (in Japanese with English abstract). Nippon Suisan Gakkaishi 62: 104-111.
    • (1996) Nippon Suisan Gakkaishi , vol.62 , pp. 104-111
    • Imai, C.1    Tsukamasa, Y.2    Sugiyama, M.3    Minegishi, Y.4    Shimizu, Y.5
  • 7
    • 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 SH, Watabe S (2003) 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. J Agric Food Chem 51: 4089-4095.
    • (2003) J Agric Food Chem , vol.51 , pp. 4089-4095
    • Fukushima, H.1    Yoon, S.H.2    Watabe, S.3
  • 8
    • 85004503526 scopus 로고
    • Formation of polymeric molecules of protein resulting from intermolecular SS bonds formed during the gel formation of carp actomyosin by heating (in Japanese with English abstract)
    • Itoh Y, Yoshinaka R, Ikeda S (1980) Formation of polymeric molecules of protein resulting from intermolecular SS bonds formed during the gel formation of carp actomyosin by heating (in Japanese with English abstract). Nippon Suisan Gakkaishi 46: 621-624.
    • (1980) Nippon Suisan Gakkaishi , vol.46 , pp. 621-624
    • Itoh, Y.1    Yoshinaka, R.2    Ikeda, S.3
  • 9
    • 84880625113 scopus 로고    scopus 로고
    • Incorporation of dansyl glutamine into muscle protein during incubation of fish flesh sol at 30 °C
    • Hossain SMZ, Ito T, Kanoh S, Niwa E (1998) Incorporation of dansyl glutamine into muscle protein during incubation of fish flesh sol at 30 °C. Fish Res 44: 95-98.
    • (1998) Fish Res , vol.44 , pp. 95-98
    • Hossain, S.M.Z.1    Ito, T.2    Kanoh, S.3    Niwa, E.4
  • 10
    • 38949160438 scopus 로고    scopus 로고
    • Discards in large-scale set net in Tateyama Bay (in Japanese with English abstract)
    • Akiyama S (2007) Discards in large-scale set net in Tateyama Bay (in Japanese with English abstract). Nippon Suisan Gakkaishi 73: 1103-1108.
    • (2007) Nippon Suisan Gakkaishi , vol.73 , pp. 1103-1108
    • Akiyama, S.1
  • 11
    • 85004488423 scopus 로고
    • Species variations in the gel-forming characteristics of fish meat paste (in Japanese with English abstract)
    • Shimizu Y, Machida R, Takenami S (1981) Species variations in the gel-forming characteristics of fish meat paste (in Japanese with English abstract). Nippon Suisan Gakkaishi 47: 95-104.
    • (1981) Nippon Suisan Gakkaishi , vol.47 , pp. 95-104
    • Shimizu, Y.1    Machida, R.2    Takenami, S.3
  • 12
    • 21144480080 scopus 로고
    • Comparison of reactivity of transglutaminase to various fish actomyosins
    • Araki H, Seki N (1993) Comparison of reactivity of transglutaminase to various fish actomyosins. Nippon Suisan Gakkaishi 59: 711-716.
    • (1993) Nippon Suisan Gakkaishi , vol.59 , pp. 711-716
    • Araki, H.1    Seki, N.2
  • 13
    • 4644370457 scopus 로고    scopus 로고
    • Characteristics and gel properties of muscles from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) caught in Thailand
    • Chaijan M, Benjakul S, Visessanguan W, Faustman C (2004) Characteristics and gel properties of muscles from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) caught in Thailand. Food Res Intern 37: 1021-1030.
    • (2004) Food Res Intern , vol.37 , pp. 1021-1030
    • Chaijan, M.1    Benjakul, S.2    Visessanguan, W.3    Faustman, C.4
  • 14
    • 77956122808 scopus 로고    scopus 로고
    • Gel properties of red tilapia surimi: effects of setting condition, fish freshness and frozen storage
    • Mahawanich T, Lekhavichitr J, Duangmal K (2010) Gel properties of red tilapia surimi: effects of setting condition, fish freshness and frozen storage. Int J Food Sci Technol 45: 1777-1786.
    • (2010) Int J Food Sci Technol , vol.45 , pp. 1777-1786
    • Mahawanich, T.1    Lekhavichitr, J.2    Duangmal, K.3
  • 15
    • 0012388642 scopus 로고
    • Effect of temperature on the rate for the setting of meat pastes from Alaska pollack, white croaker and tilapia (in Japanese with English abstract)
    • Katoh N, Hashimoto A, Nozaki H, Arai K (1984) Effect of temperature on the rate for the setting of meat pastes from Alaska pollack, white croaker and tilapia (in Japanese with English abstract). Nippon Suisan Gakkaishi 50: 2103-2108.
    • (1984) Nippon Suisan Gakkaishi , vol.50 , pp. 2103-2108
    • Katoh, N.1    Hashimoto, A.2    Nozaki, H.3    Arai, K.4
  • 16
    • 85008094000 scopus 로고
    • Temperature-dependent changes in gel strength and myosin heavy chain of salt-ground meat from walleye pollack during setting (in Japanese with English abstract)
    • Numakura T, Kimura I, Toyoda K, Fujita T (1990) Temperature-dependent changes in gel strength and myosin heavy chain of salt-ground meat from walleye pollack during setting (in Japanese with English abstract). Nippon Suisan Gakkaishi 56: 2035-2043.
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 2035-2043
    • Numakura, T.1    Kimura, I.2    Toyoda, K.3    Fujita, T.4
  • 17
    • 85008091961 scopus 로고
    • Changes in myosin heavy chain and gel forming ability of salt-ground meat from hoki (in Japanese with English abstract)
    • Lee N-H, Seki N, Kato N, Nakagawa N, Terui S, Ken-ichi A (1990) Changes in myosin heavy chain and gel forming ability of salt-ground meat from hoki (in Japanese with English abstract). Nippon Suisan Gakkaishi 56: 2093-2101.
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 2093-2101
    • Lee, N.-H.1    Seki, N.2    Kato, N.3    Nakagawa, N.4    Terui, S.5    Ken-Ichi, A.6
  • 18
    • 84893592478 scopus 로고
    • ε-(γ-Glutamyl)lysine crosslink formation in sardine myofibril sol during setting at 25 °C
    • Tsukamasa Y, Sato K, Shimizu Y, Imai C, Sugiyama M et al (1993) ε-(γ-Glutamyl)lysine crosslink formation in sardine myofibril sol during setting at 25 °C. J Food Sci 58: 785-787.
    • (1993) J Food Sci , vol.58 , pp. 785-787
    • Tsukamasa, Y.1    Sato, K.2    Shimizu, Y.3    Imai, C.4    Sugiyama, M.5
  • 19
    • 0034866261 scopus 로고    scopus 로고
    • Surimi of fish species from the Gulf of Mexico: evaluation of the setting phenomenon
    • Morales OG, Ramírez JA, Vivanco DI, Vazquez M (2001) Surimi of fish species from the Gulf of Mexico: evaluation of the setting phenomenon. Food Chem 75: 43-48.
    • (2001) Food Chem , vol.75 , pp. 43-48
    • Morales, O.G.1    Ramírez, J.A.2    Vivanco, D.I.3    Vazquez, M.4
  • 20
    • 77954793458 scopus 로고    scopus 로고
    • Gel-forming characteristics of surimi from white croaker under the inhibition of the polymerization and degradation of protein
    • Phu NV, Morioka K, Itoh Y (2010) Gel-forming characteristics of surimi from white croaker under the inhibition of the polymerization and degradation of protein. J Biol Sci 10: 432-439.
    • (2010) J Biol Sci , vol.10 , pp. 432-439
    • Phu, N.V.1    Morioka, K.2    Itoh, Y.3
  • 21
    • 85008030175 scopus 로고
    • Thermostablity of fish myofibrillar Ca-ATPase and adaptation to environmental temperature (in Japanese with English abstract)
    • Hashimoto A, Kobayashi A, Arai K (1982) Thermostablity of fish myofibrillar Ca-ATPase and adaptation to environmental temperature (in Japanese with English abstract). Nippon Suisan Gakkaishi 48: 671-684.
    • (1982) Nippon Suisan Gakkaishi , vol.48 , pp. 671-684
    • Hashimoto, A.1    Kobayashi, A.2    Arai, K.3
  • 22
    • 0000724738 scopus 로고
    • The relative stabilities of the skeletal-muscle myosins of some animals
    • Connell JJ (1961) The relative stabilities of the skeletal-muscle myosins of some animals. Biochem J 80: 503-509.
    • (1961) Biochem J , vol.80 , pp. 503-509
    • Connell, J.J.1
  • 23
    • 0028913571 scopus 로고
    • Differences in the thermal stability of acclimation temperature-associated types of carp myosin and its rod on differential scanning calorimetry
    • Nakaya M, Watabe S, Ooi T (1995) Differences in the thermal stability of acclimation temperature-associated types of carp myosin and its rod on differential scanning calorimetry. Biochemistry 34: 3114-3120.
    • (1995) Biochemistry , vol.34 , pp. 3114-3120
    • Nakaya, M.1    Watabe, S.2    Ooi, T.3
  • 24
    • 0031461886 scopus 로고    scopus 로고
    • Carp expresses fast skeletal isoforms with altered motor functions and structural stabilities to compensate for changes in environmental temperature
    • Watabe S, Hirayama Y, Nakaya M, Kakinuma M, Kikuchi K, Guo XF, Kanoh S, Chaen S, Ooi T (1998) Carp expresses fast skeletal isoforms with altered motor functions and structural stabilities to compensate for changes in environmental temperature. J Therm Biol 22: 375-390.
    • (1998) J Therm Biol , vol.22 , pp. 375-390
    • Watabe, S.1    Hirayama, Y.2    Nakaya, M.3    Kakinuma, M.4    Kikuchi, K.5    Guo, X.F.6    Kanoh, S.7    Chaen, S.8    Ooi, T.9
  • 25
    • 85008099364 scopus 로고
    • Influencing factors on changes in myosin heavy chain and jelly strength of salted meat paste from Alaska pollack during setting (in Japanese with English abstract)
    • Nishimoto S, Hashimoto A, Seki N, Kimura I, Toyoda K, Fujita T, Arai K (1987) Influencing factors on changes in myosin heavy chain and jelly strength of salted meat paste from Alaska pollack during setting (in Japanese with English abstract). Nippon Suisan Gakkaishi 53: 2011-2020.
    • (1987) Nippon Suisan Gakkaishi , vol.53 , pp. 2011-2020
    • Nishimoto, S.1    Hashimoto, A.2    Seki, N.3    Kimura, I.4    Toyoda, K.5    Fujita, T.6    Arai, K.7
  • 26
    • 0006052577 scopus 로고
    • Effects of monovalent cations on cross-linking of myosin in suwari gels from walleye pollack
    • Wan J, Miura J, Seki N (1992) Effects of monovalent cations on cross-linking of myosin in suwari gels from walleye pollack. Nippon Suisan Gakkaishi 58: 583-590.
    • (1992) Nippon Suisan Gakkaishi , vol.58 , pp. 583-590
    • Wan, J.1    Miura, J.2    Seki, N.3
  • 27
    • 21144474056 scopus 로고
    • Effect of salts on transglutaminase-mediated cross-linking of myosin in suwari gel from walleye pollack (in Japanese with English abstract)
    • Wan J, Seki N (1992) Effect of salts on transglutaminase-mediated cross-linking of myosin in suwari gel from walleye pollack (in Japanese with English abstract). Nippon Suisan Gakkaishi 58: 2181-2187.
    • (1992) Nippon Suisan Gakkaishi , vol.58 , pp. 2181-2187
    • Wan, J.1    Seki, N.2
  • 28
    • 85007905278 scopus 로고
    • Effect of calcium ion concentration on the gelling properties and transglutaminase activity of walleye pollack surimi paste
    • Wan J, Kimura I, Satake M, Seki N (1994) Effect of calcium ion concentration on the gelling properties and transglutaminase activity of walleye pollack surimi paste. Nippon Suisan Gakkaishi 60: 107-113.
    • (1994) Nippon Suisan Gakkaishi , vol.60 , pp. 107-113
    • Wan, J.1    Kimura, I.2    Satake, M.3    Seki, N.4
  • 29
    • 0034852154 scopus 로고    scopus 로고
    • Contribution of the polymerization of protein by disulfide bonding to increased gel strength of walleye pollack surimi gel with preheating time
    • Hossain MI, Itoh Y, Morioka K, Obatake A (2001) Contribution of the polymerization of protein by disulfide bonding to increased gel strength of walleye pollack surimi gel with preheating time. Fish Sci 67: 710-717.
    • (2001) Fish Sci , vol.67 , pp. 710-717
    • Hossain, M.I.1    Itoh, Y.2    Morioka, K.3    Obatake, A.4
  • 30
    • 0039890179 scopus 로고    scopus 로고
    • Effect of pH on the gelation of walleye pollack surimi and carp actomyosin pastes
    • Ni S, Nozawa H, Seki N (2001) Effect of pH on the gelation of walleye pollack surimi and carp actomyosin pastes. Fish Sci 67: 920-927.
    • (2001) Fish Sci , vol.67 , pp. 920-927
    • Ni, S.1    Nozawa, H.2    Seki, N.3
  • 32
    • 27944437909 scopus 로고    scopus 로고
    • Myofibrillar proteolysis by myofibril-bound serine protease from white croaker Argyrosomus argentatus
    • Ohkubo M, Osatomi K, Hara K, Ishihara T, Aranishi F (2005) Myofibrillar proteolysis by myofibril-bound serine protease from white croaker Argyrosomus argentatus. Fish Sci 71: 1143-1148.
    • (2005) Fish Sci , vol.71 , pp. 1143-1148
    • Ohkubo, M.1    Osatomi, K.2    Hara, K.3    Ishihara, T.4    Aranishi, F.5
  • 33
    • 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, Watabe S (2003) Thermal effects on fast skeletal myosins from Alaska pollock, white croaker, and rabbit in relation to gel formation. J Food Sci 68: 1573-1577.
    • (2003) J Food Sci , vol.68 , pp. 1573-1577
    • Fukushima, H.1    Satoh, Y.2    Nakaya, M.3    Ishizaki, S.4    Watabe, S.5
  • 34
    • 0036697486 scopus 로고    scopus 로고
    • Leptocephalus larvae of Pterothrissus gissu collected from the Kuroshio-Oyashio transition region of the western North Pacific, with comments on its metamorphosis
    • Tsukamoto Y (2002) Leptocephalus larvae of Pterothrissus gissu collected from the Kuroshio-Oyashio transition region of the western North Pacific, with comments on its metamorphosis. Ichthyol Res 49: 267-269.
    • (2002) Ichthyol Res , vol.49 , pp. 267-269
    • Tsukamoto, Y.1
  • 35
    • 84880631335 scopus 로고    scopus 로고
    • Habitat depth of deepsea bonefish Pterothrissus gissu Hilgendorf in Sagami Bay (in Japanese with English abstract)
    • Mitani I (2000) Habitat depth of deepsea bonefish Pterothrissus gissu Hilgendorf in Sagami Bay (in Japanese with English abstract). Bull Kanagawa Pref Fish Res Inst 5: 65-69.
    • (2000) Bull Kanagawa Pref Fish Res Inst , vol.5 , pp. 65-69
    • Mitani, I.1
  • 36
    • 85008100739 scopus 로고
    • The speed of lowering in freshness of fishes in several waters and the effect of the habitat temperature on the speed
    • Tsuchimoto M, Misima T, Utsugi T, Kitajima S, Yada S, Senta T, Yasuda M (1986) The speed of lowering in freshness of fishes in several waters and the effect of the habitat temperature on the speed. Nippon Suisan Gakkaishi 52: 1431-1441.
    • (1986) Nippon Suisan Gakkaishi , vol.52 , pp. 1431-1441
    • Tsuchimoto, M.1    Misima, T.2    Utsugi, T.3    Kitajima, S.4    Yada, S.5    Senta, T.6    Yasuda, M.7
  • 38
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall A, Bardawill C, David M (1949) Determination of serum proteins by means of the biuret reaction. J Biol Chem 177: 751-766.
    • (1949) J Biol Chem , vol.177 , pp. 751-766
    • Gornall, A.1    Bardawill, C.2    David, M.3
  • 39
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber K, Osborn M (1969) The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem 244: 4406-4412.
    • (1969) J Biol Chem , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 40
    • 0000990096 scopus 로고    scopus 로고
    • Determination of primary structure of heavy meromyosin region of walleye pollack myosin heavy chain by cDNA cloning
    • Ojima T, Togashi N, Inoue A, Amauchi A, Togashi M, Watabe S, Nishita K (1998) Determination of primary structure of heavy meromyosin region of walleye pollack myosin heavy chain by cDNA cloning. Fish Sci 64: 812-819.
    • (1998) Fish Sci , vol.64 , pp. 812-819
    • Ojima, T.1    Togashi, N.2    Inoue, A.3    Amauchi, A.4    Togashi, M.5    Watabe, S.6    Nishita, K.7
  • 41
    • 18744369369 scopus 로고    scopus 로고
    • cDNA cloning of myosin heavy chain from white croaker fast skeletal muscle and characterization of its complete primary structure
    • Yoon SH, Kakinuma M, Hirayama Y, Yamamoto T, Watabe S (2000) cDNA cloning of myosin heavy chain from white croaker fast skeletal muscle and characterization of its complete primary structure. Fish Sci 66: 1163-1171.
    • (2000) Fish Sci , vol.66 , pp. 1163-1171
    • Yoon, S.H.1    Kakinuma, M.2    Hirayama, Y.3    Yamamoto, T.4    Watabe, S.5
  • 42
    • 85006173213 scopus 로고
    • Purification and characterization of a tissue-type transglutaminase from red sea bream (Pagrus major)
    • Yasueda H, Kumazawa Y, Motoki M (1994) Purification and characterization of a tissue-type transglutaminase from red sea bream (Pagrus major). Biosci Biotechnol Biochem 58: 2041-2045.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 2041-2045
    • Yasueda, H.1    Kumazawa, Y.2    Motoki, M.3
  • 43
    • 84860881051 scopus 로고    scopus 로고
    • cDNA cloning and primary structure analysis of transglutaminase from bluefin tuna Thunnus orientalis
    • Ikeguchi K, Kaneko G, Watabe S (2012) cDNA cloning and primary structure analysis of transglutaminase from bluefin tuna Thunnus orientalis. Fish Sci 78: 667-674.
    • (2012) Fish Sci , vol.78 , pp. 667-674
    • Ikeguchi, K.1    Kaneko, G.2    Watabe, S.3
  • 44
    • 0031452970 scopus 로고    scopus 로고
    • Partial purification and characterization of six transglutaminases from ordinary muscles of various fishes and marine invertebrates
    • Nozawa H, Mamegoshi S, Seki N (1997) Partial purification and characterization of six transglutaminases from ordinary muscles of various fishes and marine invertebrates. Comp Biochem Physiol B Biochem Mol Biol 118: 313-317.
    • (1997) Comp Biochem Physiol B Biochem Mol Biol , vol.118 , pp. 313-317
    • Nozawa, H.1    Mamegoshi, S.2    Seki, N.3


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