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Volumn , Issue , 2009, Pages 173-213

Differential Scanning Calorimetry

Author keywords

Differential scanning calorimetry (DSC), established measuring method; DSC application investigating quality and safety; DSC curve, plot of heat flow against temperature; DSC for analysing phase changes; First applications of DSC on fish muscle and other seafood; Heat flux differential scanning calorimeter class of heat exchanging calorimeters; Power compensation DSC, PerkinElmer DSC 7; Suitability of DSC in quality and safety assessment in fish processing

Indexed keywords

CALORIMETERS; FISH; HEAT FLUX;

EID: 78650197748     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9781444322668.ch8     Document Type: Chapter
Times cited : (14)

References (160)
  • 1
    • 0035031352 scopus 로고    scopus 로고
    • Change of K-value and water state of yellowfin tuna Thunnus albacares meat stored in a wide temperature range (20 to -84 °C)
    • Agustini, T.W., Suzuki, T., Hagiwara, T., Ishizaki, S., Tanaka, M. and Takai, R. (2001) Change of K-value and water state of yellowfin tuna Thunnus albacares meat stored in a wide temperature range (20 to -84 °C). Fisheries Science 67: 306-313.
    • (2001) Fisheries Science , vol.67 , pp. 306-313
    • Agustini, T.W.1    Suzuki, T.2    Hagiwara, T.3    Ishizaki, S.4    Tanaka, M.5    Takai, R.6
  • 4
    • 0036097930 scopus 로고    scopus 로고
    • Changes in the texture and structure of cod and haddock fillets during frozen storage
    • Badii, F. and Howell, N.K. (2002a) Changes in the texture and structure of cod and haddock fillets during frozen storage. Food Hydrocolloids 16: 313-319.
    • (2002) Food Hydrocolloids , vol.16 , pp. 313-319
    • Badii, F.1    Howell, N.K.2
  • 5
    • 0036150757 scopus 로고    scopus 로고
    • A comparison of biochemical changes in cod (Gadus morhua) and haddock (Melanogrammus aeglefinus) fillets during frozen storage
    • Badii, F. and Howell, N.K. (2002b) A comparison of biochemical changes in cod (Gadus morhua) and haddock (Melanogrammus aeglefinus) fillets during frozen storage. Journal of the Science of Food and Agriculture 82: 87-97.
    • (2002) Journal of the Science of Food and Agriculture , vol.82 , pp. 87-97
    • Badii, F.1    Howell, N.K.2
  • 6
    • 0037467080 scopus 로고    scopus 로고
    • Elucidation of the effect of formaldehyde and lipids on frozen stored cod collagen by FT-Raman spectroscopy and differential scanning calorimetry
    • Badii, F. and Howell, N.K. (2003) Elucidation of the effect of formaldehyde and lipids on frozen stored cod collagen by FT-Raman spectroscopy and differential scanning calorimetry. Journal of Agricultural and Food Chemistry 51: 1440-1446.
    • (2003) Journal of Agricultural and Food Chemistry , vol.51 , pp. 1440-1446
    • Badii, F.1    Howell, N.K.2
  • 7
    • 32944474540 scopus 로고    scopus 로고
    • Fish gelatin: structure, gelling properties and interaction with egg albumen proteins
    • Badii, F. and Howell, N.K. (2006) Fish gelatin: structure, gelling properties and interaction with egg albumen proteins. Food Hydrocolloids 20: 630-640.
    • (2006) Food Hydrocolloids , vol.20 , pp. 630-640
    • Badii, F.1    Howell, N.K.2
  • 8
    • 0000126814 scopus 로고    scopus 로고
    • Studies on differential scanning calorimetry and thermogravimetry of tilapia (Oreochromis nilotica) surimi, surimi/starch and surimi/ starch/carrageenan systems
    • Barreto, P.L.M., Beirao, L.H., Soldi, M.S. and Soldi, V. (2000) Studies on differential scanning calorimetry and thermogravimetry of tilapia (Oreochromis nilotica) surimi, surimi/starch and surimi/ starch/carrageenan systems. Journal of Food Science Technology 37: 265-271.
    • (2000) Journal of Food Science Technology , vol.37 , pp. 265-271
    • Barreto, P.L.M.1    Beirao, L.H.2    Soldi, M.S.3    Soldi, V.4
  • 9
    • 84987367565 scopus 로고
    • Thermal denaturation of hake (Merluccius hubbsi) myofibrillar proteins. a differential scanning calorimetric and electrophoretic study
    • Beas, V.E., Wagner, J.R., Crupkin, M. and Anon, M.C. (1990) Thermal denaturation of hake (Merluccius hubbsi) myofibrillar proteins. a differential scanning calorimetric and electrophoretic study. Journal of Food Science 55: 683-686, 696.
    • (1990) Journal of Food Science , vol.55
    • Beas, V.E.1    Wagner, J.R.2    Crupkin, M.3    Anon, M.C.4
  • 10
    • 84985225012 scopus 로고
    • Thermal denaturation in fish muscle protein during gelling: effect of spawning condition
    • Beas, V.E., Wagner, J.R., Anon, M.C. and Crupkin, M. (1991) Thermal denaturation in fish muscle protein during gelling: effect of spawning condition. Journal of Food Science 56: 281-284.
    • (1991) Journal of Food Science , vol.56 , pp. 281-284
    • Beas, V.E.1    Wagner, J.R.2    Anon, M.C.3    Crupkin, M.4
  • 11
    • 0042562161 scopus 로고    scopus 로고
    • Thermophysical properties of silver hake and mackerel surimi at cooking temperatures
    • Belibagli, K.B., Speers, R.A. and Paulson, A.T. (2003) Thermophysical properties of silver hake and mackerel surimi at cooking temperatures. Journal of Food Engineering 60: 439-448.
    • (2003) Journal of Food Engineering , vol.60 , pp. 439-448
    • Belibagli, K.B.1    Speers, R.A.2    Paulson, A.T.3
  • 12
    • 0000386238 scopus 로고
    • Recent developments in bio-calorimetry with micro-DSC
    • Benoist, L. (1990) Recent developments in bio-calorimetry with micro-DSC. Thermochimica Acta 163: 111-116.
    • (1990) Thermochimica Acta , vol.163 , pp. 111-116
    • Benoist, L.1
  • 13
    • 33845339636 scopus 로고    scopus 로고
    • Influence of freezing and of frozen storage on the specific heat capacity of trout and herring fillet
    • gen.Klass
    • Beyrer, M. and Rüsch, M. gen. Klass. (2007) Influence of freezing and of frozen storage on the specific heat capacity of trout and herring fillet. European Food Research and Technology 224: 349-353.
    • (2007) European Food Research and Technology , vol.224 , pp. 349-353
    • Beyrer, M.1    Rüsch, M.2
  • 14
    • 0001192391 scopus 로고
    • Differential scanning calorimetry in food research - a review
    • Biliarderis, C.G. (1983) Differential scanning calorimetry in food research - a review. Food Chemistry 10: 239-265.
    • (1983) Food Chemistry , vol.10 , pp. 239-265
    • Biliarderis, C.G.1
  • 15
    • 85052700473 scopus 로고    scopus 로고
    • Thermal denaturation and coagulation of proteins
    • S. Damodaran and A. Paraf (Eds), Marcel Dekker, New York, Basel and Hong Kong
    • Boye, J.I., Ma, C.-Y. and Harwalkar, V.R. (1997) Thermal denaturation and coagulation of proteins. In: S. Damodaran and A. Paraf (Eds) Food Proteins and their Applications. Marcel Dekker, New York, Basel and Hong Kong, pp. 25-56.
    • (1997) Food Proteins and their Applications , pp. 25-56
    • Boye, J.I.1    Ma, C.-Y.2    Harwalkar, V.R.3
  • 16
    • 0033051276 scopus 로고    scopus 로고
    • Glass transition values of muscle tissue
    • Brake, N.C. and Fennema, O.R. (1999) Glass transition values of muscle tissue. Journal of Food Science 64: 10-15.
    • (1999) Journal of Food Science , vol.64 , pp. 10-15
    • Brake, N.C.1    Fennema, O.R.2
  • 17
    • 0025281866 scopus 로고
    • Study of strong to ultratight protein interactions using differential scanning calorimetry
    • Brandts, J.F. and Lin, L.N. (1990) Study of strong to ultratight protein interactions using differential scanning calorimetry. Biochemistry 29: 6927-6940.
    • (1990) Biochemistry , vol.29 , pp. 6927-6940
    • Brandts, J.F.1    Lin, L.N.2
  • 18
    • 0026908646 scopus 로고
    • Thermodynamic substantiation of water-bridged collagen structure
    • Burjanadze T.V. (1992) Thermodynamic substantiation of water-bridged collagen structure. Biopolymers 32: 941-949.
    • (1992) Biopolymers , vol.32 , pp. 941-949
    • Burjanadze, T.V.1
  • 19
    • 0036896756 scopus 로고    scopus 로고
    • Extractability and thermal stability of frozen hake (Merluccius merluccius) fillets stored at -10 and -30 °C
    • Careche, M., del Mazo, M.L. and Fernández-Martín, F. (2002) Extractability and thermal stability of frozen hake (Merluccius merluccius) fillets stored at -10 and -30 °C. Journal of the Science of Food and Agriculture 82: 1791-1799.
    • (2002) Journal of the Science of Food and Agriculture , vol.82 , pp. 1791-1799
    • Careche, M.1    Del Mazo, M.L.2    Fernández-Martín, F.3
  • 20
    • 4143129281 scopus 로고    scopus 로고
    • Spectroscopic and calorimetric methods for characterizing proteins and peptides
    • P.R. Carey (Ed), Academic Press, San Diego
    • Carey, P.P. and Surewicz, W.K. (1996) Spectroscopic and calorimetric methods for characterizing proteins and peptides. In: P.R. Carey (Ed) Protein Engineering and Design. Academic Press, San Diego, pp. 233-263.
    • (1996) Protein Engineering and Design , pp. 233-263
    • Carey, P.P.1    Surewicz, W.K.2
  • 21
    • 0011762658 scopus 로고    scopus 로고
    • Studies on thermal denaturation of fish myoglobins using differential scanning calorimetry, circular dichroism, and tryptophan flourescence
    • Chanthai, S., Ogawa, M., Tamiya, T. and Tsuchiya, T. (1996a) Studies on thermal denaturation of fish myoglobins using differential scanning calorimetry, circular dichroism, and tryptophan flourescence. Fisheries Science 62: 972-932.
    • (1996) Fisheries Science , vol.62 , pp. 932-972
    • Chanthai, S.1    Ogawa, M.2    Tamiya, T.3    Tsuchiya, T.4
  • 22
    • 0342382548 scopus 로고    scopus 로고
    • Studies on thermal denaturation of fish apomyoglobins using differential scanning calorimetry, circular dichroism, and flourescence
    • Chanthai, S., Ogawa, M., Tamiya, T. and Tsuchiya, T. (1996b) Studies on thermal denaturation of fish apomyoglobins using differential scanning calorimetry, circular dichroism, and flourescence. Fisheries Science 62: 933-937.
    • (1996) Fisheries Science , vol.62 , pp. 933-937
    • Chanthai, S.1    Ogawa, M.2    Tamiya, T.3    Tsuchiya, T.4
  • 23
    • 0000855905 scopus 로고
    • Thermal stability and gel-forming ability of shark muscle
    • Chen, H.-H. (1995) Thermal stability and gel-forming ability of shark muscle. Journal of Food Science 60: 1237-1240.
    • (1995) Journal of Food Science , vol.60 , pp. 1237-1240
    • Chen, H.-H.1
  • 24
    • 34247610123 scopus 로고    scopus 로고
    • Changes in the thermal stability of silvertip shark (Carcharhinus albimarginatus) during frozen storage
    • Chen, H.-H. (1996) Changes in the thermal stability of silvertip shark (Carcharhinus albimarginatus) during frozen storage. Food Science 23: 56-65.
    • (1996) Food Science , vol.23 , pp. 56-65
    • Chen, H.-H.1
  • 25
    • 0040065330 scopus 로고    scopus 로고
    • Changes in freshness and gelation characteristics of small hammer-head shark during cold storage
    • Chen, H.-H., Lou, S.-N. and Chen, T.-Y. (1996a) Changes in freshness and gelation characteristics of small hammer-head shark during cold storage. Journal of the Chinese Agricultural Chemical Society 34: 174-187.
    • (1996) Journal of the Chinese Agricultural Chemical Society , vol.34 , pp. 174-187
    • Chen, H.-H.1    Lou, S.-N.2    Chen, T.-Y.3
  • 26
    • 0040658832 scopus 로고    scopus 로고
    • Biochemical properties, thermal stability and gelation properties of thresher shark (Alopias pelagicus) during frozen storage
    • Chen, H.-H., Lou, S.-N. and Chen, T.-Y. (1996b) Biochemical properties, thermal stability and gelation properties of thresher shark (Alopias pelagicus) during frozen storage. Journal of the Chinese Agricultural Chemical Society 34: 309-322.
    • (1996) Journal of the Chinese Agricultural Chemical Society , vol.34 , pp. 309-322
    • Chen, H.-H.1    Lou, S.-N.2    Chen, T.-Y.3
  • 27
    • 14344260107 scopus 로고    scopus 로고
    • Combination model for the spatial partition of surimi protein and hydroxylpropylmethylcellulose
    • Chen, H.-H., Ferng, L.-H., Chen, S.-D., Sun, W.-C. and Lee, Y.-C. (2005) Combination model for the spatial partition of surimi protein and hydroxylpropylmethylcellulose. Food Hydrocolloids 19: 761-768.
    • (2005) Food Hydrocolloids , vol.19 , pp. 761-768
    • Chen, H.-H.1    Ferng, L.-H.2    Chen, S.-D.3    Sun, W.-C.4    Lee, Y.-C.5
  • 28
    • 2442586757 scopus 로고    scopus 로고
    • Thermal stability and denaturation rate of myoglobin from various species of fish
    • Chen, L.-C., Lin, S.-B. and Chen, H.-H. (2004) Thermal stability and denaturation rate of myoglobin from various species of fish. Fisheries Science 70: 293-298.
    • (2004) Fisheries Science , vol.70 , pp. 293-298
    • Chen, L.-C.1    Lin, S.-B.2    Chen, H.-H.3
  • 29
    • 84960238836 scopus 로고    scopus 로고
    • Combined use of traditional and DSC methods in monitoring rigor mortis development of iced chub mackerel
    • Chen, T.-Y. and Kong, M.-S. (1997) Combined use of traditional and DSC methods in monitoring rigor mortis development of iced chub mackerel. Journal of the Chinese Agricultural Chemical Society 35: 333-341.
    • (1997) Journal of the Chinese Agricultural Chemical Society , vol.35 , pp. 333-341
    • Chen, T.-Y.1    Kong, M.-S.2
  • 30
    • 0031496501 scopus 로고    scopus 로고
    • Effect of fish protein, salt, sugar, and monosodium glutamate on the gelatinization of starch in fish-starch mixtures
    • Cheow, C.S. and Yu, S.Y. (1997) Effect of fish protein, salt, sugar, and monosodium glutamate on the gelatinization of starch in fish-starch mixtures. Journal of Food Processing and Preservation 21: 161-177.
    • (1997) Journal of Food Processing and Preservation , vol.21 , pp. 161-177
    • Cheow, C.S.1    Yu, S.Y.2
  • 31
    • 33747125051 scopus 로고    scopus 로고
    • Preparation and characterisation of gelatins from the skins of sin croaker (Johnius dussumieri) and shortfin scad (Decapterus macrosoma)
    • Cheow, C.S., Norizah, M.S., Kyaw, Z.Y. and Howell, N.K. (2007) Preparation and characterisation of gelatins from the skins of sin croaker (Johnius dussumieri) and shortfin scad (Decapterus macrosoma). Food Chemistry 101: 386-391.
    • (2007) Food Chemistry , vol.101 , pp. 386-391
    • Cheow, C.S.1    Norizah, M.S.2    Kyaw, Z.Y.3    Howell, N.K.4
  • 32
    • 84985280168 scopus 로고
    • Water binding and ingredient dispersion pattern effects on surimi gel texture
    • Chung, K.H. and Lee, C.M. (1991) Water binding and ingredient dispersion pattern effects on surimi gel texture. Journal of Food Science 56: 1263-1266.
    • (1991) Journal of Food Science , vol.56 , pp. 1263-1266
    • Chung, K.H.1    Lee, C.M.2
  • 33
    • 0032291854 scopus 로고    scopus 로고
    • Biochemical and biological applications of thermal analysis
    • Collet, L.A., Brown, M.E. (1998) Biochemical and biological applications of thermal analysis. Journal of Thermal Analysis 51: 693-726.
    • (1998) Journal of Thermal Analysis , vol.51 , pp. 693-726
    • Collet, L.A.1    Brown, M.E.2
  • 34
    • 0037920996 scopus 로고    scopus 로고
    • Thermodynamics of protein folding and stability
    • G. Allen (Ed), JAI Press, Greenwich, Connecticut
    • Cooper, A. (1999) Thermodynamics of protein folding and stability. In: G. Allen (Ed) Protein: A Comprehensive Treatise. JAI Press, Greenwich, Connecticut, pp. 217-270.
    • (1999) Protein: A Comprehensive Treatise , pp. 217-270
    • Cooper, A.1
  • 37
    • 29544448232 scopus 로고    scopus 로고
    • Effect of ice storage on the physicochemical and dynamic viscoelastic properties of ribbonfish (Trichiurus spp.) meat
    • Dileep, A.O., Shamasundar, B.A., Binsi, P.K., Badii, F. and Howell, N.K. (2005) Effect of ice storage on the physicochemical and dynamic viscoelastic properties of ribbonfish (Trichiurus spp.) meat. Journal of Food Science 70: E537-E545.
    • (2005) Journal of Food Science , vol.70 , pp. E537-E545
    • Dileep, A.O.1    Shamasundar, B.A.2    Binsi, P.K.3    Badii, F.4    Howell, N.K.5
  • 38
    • 0039337707 scopus 로고    scopus 로고
    • Prevention of protein denaturation of jack mackerel actomyosin (Trachurus murphyi) during frozen storage
    • Dondero, M., Araya, M. and Curotto, E. (1996) Prevention of protein denaturation of jack mackerel actomyosin (Trachurus murphyi) during frozen storage. Food Science and Technology International 2: 79-86.
    • (1996) Food Science and Technology International , vol.2 , pp. 79-86
    • Dondero, M.1    Araya, M.2    Curotto, E.3
  • 39
    • 0029198941 scopus 로고
    • Differential scanning calorimetry
    • B.A. Shirley (Ed), (Protein Stability and Folding: Theory and Practice). Humana Press, Totowa, NJ
    • Freire, E. (1995) Differential scanning calorimetry. In: B.A. Shirley (Ed) Methods in Molecular Biology, Volume 40 (Protein Stability and Folding: Theory and Practice). Humana Press, Totowa, NJ, pp. 191-218.
    • (1995) Methods in Molecular Biology , vol.40 , pp. 191-218
    • Freire, E.1
  • 40
    • 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. (2003a) Thermal effects on fast skeletal myosins from Alaska pollock, white croaker, and rabbit in relation to gel formation. Journal of Food Science 68: 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
  • 41
    • 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. (2003b) 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: 4089-4095.
    • (2003) Journal of Agricultural and Food Chemistry , vol.51 , pp. 4089-4095
    • Fukushima, H.1    Yoon, S.H.2    Watabe, S.3
  • 42
    • 84985166031 scopus 로고
    • Influence of water content on the stability of myoglobin to heat treatment
    • Hägerdal, B. and Martens, H. (1976) Influence of water content on the stability of myoglobin to heat treatment. Journal of Food Science 41: 933-937.
    • (1976) Journal of Food Science , vol.41 , pp. 933-937
    • Hägerdal, B.1    Martens, H.2
  • 43
    • 0025737309 scopus 로고
    • Calorimetric analysis of antifreeze glycoproteins of the polar fish, Dissostichus mawsoni
    • Hansen, T.N., DeVries, A.L. and Baust, J.G. (1991) Calorimetric analysis of antifreeze glycoproteins of the polar fish, Dissostichus mawsoni. Biochimica et Biophysica Acta 1079: 169-173.
    • (1991) Biochimica et Biophysica Acta , vol.1079 , pp. 169-173
    • Hansen, T.N.1    DeVries, A.L.2    Baust, J.G.3
  • 45
    • 0347694808 scopus 로고    scopus 로고
    • Study on the glass transition of Katsuobushi (boiled and dried bonito fish stick) by differential scanning calorimetry and dynamic mechanical analysis
    • Hashimoto, T., Hagiwara, T., Suzuki, T. and Takai, R. (2003) Study on the glass transition of Katsuobushi (boiled and dried bonito fish stick) by differential scanning calorimetry and dynamic mechanical analysis. Fisheries Science 69: 1290-1297.
    • (2003) Fisheries Science , vol.69 , pp. 1290-1297
    • Hashimoto, T.1    Hagiwara, T.2    Suzuki, T.3    Takai, R.4
  • 46
    • 11144319947 scopus 로고    scopus 로고
    • Study on the glass transition for several processed fish muscles and its protein fractions using differential scanning calorimetry
    • Hashimoto, T., Suzuki, T., Hagiwara, T. and Takai, R. (2004) Study on the glass transition for several processed fish muscles and its protein fractions using differential scanning calorimetry. Fisheries Science 70: 1144-1152.
    • (2004) Fisheries Science , vol.70 , pp. 1144-1152
    • Hashimoto, T.1    Suzuki, T.2    Hagiwara, T.3    Takai, R.4
  • 48
    • 84985273101 scopus 로고
    • Differential scanning calorimetry of fish muscle: the effect of processing and species variation
    • Hastings, R.J., Rodger, G.W., Park, R., Matthews, A.D. and Anderson, E.M. (1985) Differential scanning calorimetry of fish muscle: the effect of processing and species variation. Journal of Food Science 50: 503-506, 510.
    • (1985) Journal of Food Science , vol.50
    • Hastings, R.J.1    Rodger, G.W.2    Park, R.3    Matthews, A.D.4    Anderson, E.M.5
  • 49
    • 0035141619 scopus 로고    scopus 로고
    • Effect of the addition of maltodextrins and sucrose on the ice-melting onset of minced fish muscle
    • Herrera, J.J., Pastoriza, L. and Nesvadba, P. (2001a) Effect of the addition of maltodextrins and sucrose on the ice-melting onset of minced fish muscle. Journal of the Science of Food and Agriculture 81: 305-310.
    • (2001) Journal of the Science of Food and Agriculture , vol.81 , pp. 305-310
    • Herrera, J.J.1    Pastoriza, L.2    Nesvadba, P.3
  • 50
    • 0035098279 scopus 로고    scopus 로고
    • A DSC study on the effects of various maltodextrins and sucrose on protein changes in frozen-stored minced blue whiting muscle
    • Herrera, J.J., Pastoriza, L. and Sampedro, G. (2001b) A DSC study on the effects of various maltodextrins and sucrose on protein changes in frozen-stored minced blue whiting muscle. Journal of the Science of Food and Agriculture 81: 377-384.
    • (2001) Journal of the Science of Food and Agriculture , vol.81 , pp. 377-384
    • Herrera, J.J.1    Pastoriza, L.2    Sampedro, G.3
  • 51
    • 40549089675 scopus 로고    scopus 로고
    • Entwicklung einer einfachen und schnellen Analysenmethode für Kohlenmonoxid in Fisch - Teil 2: Methodenoptimierung
    • Heyer, H. and Schubring, R. (2005) Entwicklung einer einfachen und schnellen Analysenmethode für Kohlenmonoxid in Fisch - Teil 2: Methodenoptimierung. Informationen aus der Fischereiforschung 52: 106-114.
    • (2005) Informationen aus der Fischereiforschung , vol.52 , pp. 106-114
    • Heyer, H.1    Schubring, R.2
  • 54
    • 0042303840 scopus 로고    scopus 로고
    • Effect of proteolytic squid protein hydrolysate on the state of water and dehydration-induced denaturation of lizard fish myofibrillar protein
    • Hossain, A., Ishihara, T., Hara, K., Osatomi, K., Khan, A. and Nozaki, Y. (2003a) Effect of proteolytic squid protein hydrolysate on the state of water and dehydration-induced denaturation of lizard fish myofibrillar protein. Journal of Agricultural and Food Chemistry 51: 4769-4774.
    • (2003) Journal of Agricultural and Food Chemistry , vol.51 , pp. 4769-4774
    • Hossain, A.1    Ishihara, T.2    Hara, K.3    Osatomi, K.4    Khan, A.5    Nozaki, Y.6
  • 55
  • 57
    • 22144478600 scopus 로고    scopus 로고
    • Fish fast skeletal muscle tropomyosins show species-specific thermal stability
    • Huang, M.C. and Ochiai, Y. (2005) Fish fast skeletal muscle tropomyosins show species-specific thermal stability. Comparative Biochemistry and Physiology B 141: 461-471.
    • (2005) Comparative Biochemistry and Physiology B , vol.141 , pp. 461-471
    • Huang, M.C.1    Ochiai, Y.2
  • 58
    • 0030444429 scopus 로고    scopus 로고
    • Thawing, refreezing and frozen storage effects on muscle functionality and sensory attributes of frozen cod (Gadus morhua)
    • Hurling, R. and McArthur, H. (1996) Thawing, refreezing and frozen storage effects on muscle functionality and sensory attributes of frozen cod (Gadus morhua). Journal of Food Science 61: 1289-1296.
    • (1996) Journal of Food Science , vol.61 , pp. 1289-1296
    • Hurling, R.1    McArthur, H.2
  • 59
    • 0030944762 scopus 로고    scopus 로고
    • Glass transition of tuna flesh at low temperature and effects of salt and moisture
    • Inoue, C. and Ishikawa, M. (1997) Glass transition of tuna flesh at low temperature and effects of salt and moisture. Journal of Food Science 62: 496-499.
    • (1997) Journal of Food Science , vol.62 , pp. 496-499
    • Inoue, C.1    Ishikawa, M.2
  • 61
    • 0038435499 scopus 로고    scopus 로고
    • Sorption isotherms and glass transition temperatures of fish protein hydrolysates with different degrees of hydrolysis
    • Jardim, D.C.P., Candido, L.M.B. and Netto, F.M. (1999) Sorption isotherms and glass transition temperatures of fish protein hydrolysates with different degrees of hydrolysis. International Journal of Food Properties 2: 227-242.
    • (1999) International Journal of Food Properties , vol.2 , pp. 227-242
    • Jardim, D.C.P.1    Candido, L.M.B.2    Netto, F.M.3
  • 62
    • 0242654982 scopus 로고    scopus 로고
    • Effect of storage conditions on differential scanning calorimetry profiles from thawed cod muscle
    • Jensen, K.N. and Jørgensen, B.M. (2003) Effect of storage conditions on differential scanning calorimetry profiles from thawed cod muscle. Lebensmittel-Wissenschaft und -Technologie 36: 807-812.
    • (2003) Lebensmittel-Wissenschaft und -Technologie , vol.36 , pp. 807-812
    • Jensen, K.N.1    Jørgensen, B.M.2
  • 63
    • 0037244953 scopus 로고    scopus 로고
    • Low-temperature transitions in cod and tuna determined by differential scanning calorimetry
    • Jensen, K.N., Jørgensen, B.M. and Nielsen, J. (2003) Low-temperature transitions in cod and tuna determined by differential scanning calorimetry. Lebensmittel-Wissenschaft und -Technologie 36: 369-374.
    • (2003) Lebensmittel-Wissenschaft und -Technologie , vol.36 , pp. 369-374
    • Jensen, K.N.1    Jørgensen, B.M.2    Nielsen, J.3
  • 65
    • 0242405996 scopus 로고    scopus 로고
    • Effect of enzymatic fish protein hydrolysate from fish scrap on the state of water and denaturation of lizard fish (Saurida wanieso) myofibrils during dehydration
    • Khan, M.A., Hossain, M.A., Hara, K., Osatomi, K., Ishihara, T. and Nozaki, Y. (2003) Effect of enzymatic fish protein hydrolysate from fish scrap on the state of water and denaturation of lizard fish (Saurida wanieso) myofibrils during dehydration. Food Science and Technology Research 9: 257-263.
    • (2003) Food Science and Technology Research , vol.9 , pp. 257-263
    • Khan, M.A.1    Hossain, M.A.2    Hara, K.3    Osatomi, K.4    Ishihara, T.5    Nozaki, Y.6
  • 66
    • 0001384663 scopus 로고
    • Effects of freeze-thaw abuse on the viscosity and gel-forming properties of surimi from two species
    • Kim, B.Y., Hamann, D.D., Lanier, T.C. and Wu, M.C. (1986) Effects of freeze-thaw abuse on the viscosity and gel-forming properties of surimi from two species. Journal of Food Science 51: 951-956, 1004.
    • (1986) Journal of Food Science , vol.51
    • Kim, B.Y.1    Hamann, D.D.2    Lanier, T.C.3    Wu, M.C.4
  • 67
    • 4444221441 scopus 로고    scopus 로고
    • Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus)
    • Kittiphattanabawon, P., Benjakul, S., Visessanguan, W., Nagai, T. and Tanaka, M. (2005) Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus). Food Chemistry 89: 363-372.
    • (2005) Food Chemistry , vol.89 , pp. 363-372
    • Kittiphattanabawon, P.1    Benjakul, S.2    Visessanguan, W.3    Nagai, T.4    Tanaka, M.5
  • 68
    • 7444253960 scopus 로고    scopus 로고
    • Denaturation of tilapia myosin fragments by high hydrostatic pressure
    • Ko, W.C., Hwang, J.S., Jao, C.L. and Hsu, K.C. (2004) Denaturation of tilapia myosin fragments by high hydrostatic pressure. Journal of Food Science 69: C604-C607.
    • (2004) Journal of Food Science , vol.69 , pp. C604-C607
    • Ko, W.C.1    Hwang, J.S.2    Jao, C.L.3    Hsu, K.C.4
  • 72
    • 26844484807 scopus 로고    scopus 로고
    • Physicochemical stability of paddlefish (Polyodon spathula) meat under refrigerated and frozen storage
    • Lou, X., Wang, C., Xiong, Y.L., Wang, B., Liu, G. and Mims, S.D. (2000) Physicochemical stability of paddlefish (Polyodon spathula) meat under refrigerated and frozen storage. Journal of Aquatic Food Product Technology 9: 27-39.
    • (2000) Journal of Aquatic Food Product Technology , vol.9 , pp. 27-39
    • Lou, X.1    Wang, C.2    Xiong, Y.L.3    Wang, B.4    Liu, G.5    Mims, S.D.6
  • 73
    • 0007886372 scopus 로고
    • Applications of differential scanning calorimetry in foods
    • M. Peleg and E.B. Bagley (Eds), AVI, Westport
    • Lund, D.B. (1983) Applications of differential scanning calorimetry in foods. In: M. Peleg and E.B. Bagley (Eds) Physical Properties of Foods. AVI, Westport, pp. 125-143.
    • (1983) Physical Properties of Foods , pp. 125-143
    • Lund, D.B.1
  • 74
    • 0022536537 scopus 로고
    • Determination of the state and content of water in normal avian, fish, porcine, bovine, and human lenses as studied by differential scanning calorimetry
    • Lundgren, C.H., Williams, T.R. and Nunnari, J.M. (1986) Determination of the state and content of water in normal avian, fish, porcine, bovine, and human lenses as studied by differential scanning calorimetry. Ophthalmic Research 18: 90-97.
    • (1986) Ophthalmic Research , vol.18 , pp. 90-97
    • Lundgren, C.H.1    Williams, T.R.2    Nunnari, J.M.3
  • 76
    • 0017101807 scopus 로고
    • Enthalpy changes associated with the denaturation of collagens of different imino acid content
    • Menashi, S., Finch, A., Gardner, P.J. and Ledward, D.A. (1976) Enthalpy changes associated with the denaturation of collagens of different imino acid content. Biochimica et Biophysica Acta 444: 623-625.
    • (1976) Biochimica et Biophysica Acta , vol.444 , pp. 623-625
    • Menashi, S.1    Finch, A.2    Gardner, P.J.3    Ledward, D.A.4
  • 79
    • 0000424348 scopus 로고
    • Trial determination of the ratio of myosin and actin in raw meat by differential scaning calorimetry
    • Mochizuki, Y., Mizuno, H., Ogawa, H. and Iso, N. (1995a) Trial determination of the ratio of myosin and actin in raw meat by differential scaning calorimetry. Fisheries Science 61: 723-724.
    • (1995) Fisheries Science , vol.61 , pp. 723-724
    • Mochizuki, Y.1    Mizuno, H.2    Ogawa, H.3    Iso, N.4
  • 80
    • 85008020281 scopus 로고
    • Changes of rhelogical properties of cuttlefish and squid meat by heat treatment
    • Mochizuki, Y., Mizuno, H., Ogawa, H., Ishimura, K., Tsuchiya, H. and Iso, N. (1995b) Changes of rhelogical properties of cuttlefish and squid meat by heat treatment. Fisheries Science 61: 680-683.
    • (1995) Fisheries Science , vol.61 , pp. 680-683
    • Mochizuki, Y.1    Mizuno, H.2    Ogawa, H.3    Ishimura, K.4    Tsuchiya, H.5    Iso, N.6
  • 81
    • 25844461366 scopus 로고    scopus 로고
    • Protein structural changes during preparation and storage of surimi
    • Moosavi-Nasab, M., Alli, I., Ismail, A.A. and Ngadi, M.O. (2005) Protein structural changes during preparation and storage of surimi. Journal of Food Science 70: C448-C453.
    • (2005) Journal of Food Science , vol.70 , pp. C448-C453
    • Moosavi-Nasab, M.1    Alli, I.2    Ismail, A.A.3    Ngadi, M.O.4
  • 83
    • 0000638224 scopus 로고
    • Differential scanning calorimetry of the kamaboko added with various natural high polymers
    • Niwa, E., Wang, T.-T., Kanoh, S. and Nakayama, T. (1988) Differential scanning calorimetry of the kamaboko added with various natural high polymers. Nippon Suisan Gakkaishi 54: 2139-2142.
    • (1988) Nippon Suisan Gakkaishi , vol.54 , pp. 2139-2142
    • Niwa, E.1    Wang, T.-T.2    Kanoh, S.3    Nakayama, T.4
  • 87
    • 85032068662 scopus 로고
    • Structural changes of carp myosin during heating
    • Ogawa, M., Tamiya, T. and Tsuchiya, T. (1994) Structural changes of carp myosin during heating. Fisheries Science 60: 723-727.
    • (1994) Fisheries Science , vol.60 , pp. 723-727
    • Ogawa, M.1    Tamiya, T.2    Tsuchiya, T.3
  • 88
    • 0037223980 scopus 로고    scopus 로고
    • The question of high- or lowtemperature glass transition in frozen fish. Construction of the supplemented state diagram for tuna muscle by differential scanning calorimetry
    • Orlien, V., Risbo, J., Andersen, M.L. and Skibsted, L.H. (2003) The question of high- or lowtemperature glass transition in frozen fish. Construction of the supplemented state diagram for tuna muscle by differential scanning calorimetry. Journal of Agricultural and Food Chemistry 51: 211-217.
    • (2003) Journal of Agricultural and Food Chemistry , vol.51 , pp. 211-217
    • Orlien, V.1    Risbo, J.2    Andersen, M.L.3    Skibsted, L.H.4
  • 89
    • 33751157330 scopus 로고
    • Thermal denaturation of Aulacomya ater ater (Molina) myofibrillar proteins: a differential scanning calorimetric study
    • Paredi, M.E., Tomas, M.C., Crupkin, M. and Anon, M.C. (1994) Thermal denaturation of Aulacomya ater ater (Molina) myofibrillar proteins: a differential scanning calorimetric study. Journal of Agricultural and Food Chemistry 42: 873-877.
    • (1994) Journal of Agricultural and Food Chemistry , vol.42 , pp. 873-877
    • Paredi, M.E.1    Tomas, M.C.2    Crupkin, M.3    Anon, M.C.4
  • 90
    • 84907421475 scopus 로고
    • Postmortem changes in adduktor muscles from Aulacomya ater ater (Molina) stored at 2-4 °C. A differential scanning calorimetric study
    • Paredi, M.E., Tomas, M.C., de Vido de Mattio, N., Crupkin, M. and Anon, M.C. (1995) Postmortem changes in adduktor muscles from Aulacomya ater ater (Molina) stored at 2-4 °C. A differential scanning calorimetric study. Journal of Agricultural and Food Chemistry 43: 1758-1761.
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 1758-1761
    • Paredi, M.E.1    Tomas, M.C.2    De Vido de Mattio, N.3    Crupkin, M.4    Anon, M.C.5
  • 91
    • 0000422216 scopus 로고    scopus 로고
    • Thermal denaturation of muscle proteins from male and female squid (Illex argentinus) at different sexual maturation stages. A differential scanning calorimetric study
    • Paredi, M.E., Tomas, M.C., Crupkin, M. and Anon, M.C. (1996) Thermal denaturation of muscle proteins from male and female squid (Illex argentinus) at different sexual maturation stages. A differential scanning calorimetric study. Journal of Agricultural and Food Chemistry 44: 3812-3816.
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 3812-3816
    • Paredi, M.E.1    Tomas, M.C.2    Crupkin, M.3    Anon, M.C.4
  • 92
    • 0001269595 scopus 로고    scopus 로고
    • Thermal stability of myofibrillar proteins from smooth and stiated muscled of scallop (Chlamys tehuelchus): a differential scanning calorimetric study
    • Paredi, M.E., Tomas, M.C., Anon, M.C. and Chrupkin, M. (1998) Thermal stability of myofibrillar proteins from smooth and stiated muscled of scallop (Chlamys tehuelchus): a differential scanning calorimetric study. Journal of Agricultural and Food Chemistry 46: 3971-3976.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 3971-3976
    • Paredi, M.E.1    Tomas, M.C.2    Anon, M.C.3    Chrupkin, M.4
  • 93
    • 0037070040 scopus 로고    scopus 로고
    • Thermal denaturation of myofibrillar proteins of striated and smooth adductor muscles of scallop (Zygochlamys patagonica). A differential scanning calorimetric study
    • Paredi, M.E., Tomas, M.C. and Crupkin, M. (2002) Thermal denaturation of myofibrillar proteins of striated and smooth adductor muscles of scallop (Zygochlamys patagonica). A differential scanning calorimetric study. Journal of Agricultural and Food Chemistry 50: 830-834.
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , pp. 830-834
    • Paredi, M.E.1    Tomas, M.C.2    Crupkin, M.3
  • 94
    • 84985225759 scopus 로고
    • Functional protein additives in surimi gels
    • Park, J.W. (1994) Functional protein additives in surimi gels. Journal of Food Science 59: 525-527.
    • (1994) Journal of Food Science , vol.59 , pp. 525-527
    • Park, J.W.1
  • 95
    • 0000740472 scopus 로고
    • Combined effects of phosphates and sugar or polyol on protein stabilization of fish myofibrils
    • Park, J.W. and Lanier, T.C. (1987) Combined effects of phosphates and sugar or polyol on protein stabilization of fish myofibrils. Journal of Food Science 52: 1509-1513.
    • (1987) Journal of Food Science , vol.52 , pp. 1509-1513
    • Park, J.W.1    Lanier, T.C.2
  • 96
    • 84985222628 scopus 로고
    • Scanning calorimetric behavior of tilapia myosin and actin due to processing of muscle and protein purification
    • Park, J.W. and Lanier, T.C. (1989) Scanning calorimetric behavior of tilapia myosin and actin due to processing of muscle and protein purification. Journal of Food Science 54: 49-51.
    • (1989) Journal of Food Science , vol.54 , pp. 49-51
    • Park, J.W.1    Lanier, T.C.2
  • 97
    • 84986464706 scopus 로고
    • Effects of salt and sucrose addition on thermal denaturation and aggregation of water-leached fish muscle
    • Park, J.W. and Lanier, T.C. (1990) Effects of salt and sucrose addition on thermal denaturation and aggregation of water-leached fish muscle. Journal of Food Biochemistry 14: 395-404.
    • (1990) Journal of Food Biochemistry , vol.14 , pp. 395-404
    • Park, J.W.1    Lanier, T.C.2
  • 101
    • 45349109508 scopus 로고
    • 3 generations of scanning microcalorimeters for liquids
    • Privalov, P.L. and Plotnikov, V.V. (1989) 3 generations of scanning microcalorimeters for liquids. Thermochimica Acta 139: 257-277.
    • (1989) Thermochimica Acta , vol.139 , pp. 257-277
    • Privalov, P.L.1    Plotnikov, V.V.2
  • 102
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov, P.L. and Potekhin, S.A. (1986) Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods in Enzymology 131: 4-51.
    • (1986) Methods in Enzymology , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 103
    • 0036414760 scopus 로고    scopus 로고
    • Bighead carp myosin stability to heat and frozen storage
    • Radicevic, T., Raicevic, S. and Niketic, V. (2002) Bighead carp myosin stability to heat and frozen storage. Acta Veterinaria 52: 151-161.
    • (2002) Acta Veterinaria , vol.52 , pp. 151-161
    • Radicevic, T.1    Raicevic, S.2    Niketic, V.3
  • 104
    • 0038425100 scopus 로고
    • Thermal behaviour of foods
    • Raemy, A. and Lambelet, P. (1991) Thermal behaviour of foods. Thermochimica Acta 193: 417-439.
    • (1991) Thermochimica Acta , vol.193 , pp. 417-439
    • Raemy, A.1    Lambelet, P.2
  • 105
    • 34249865663 scopus 로고    scopus 로고
    • Conformational and rheological changes in catfish myosin as affected by different acids during acid-induced unfolding and refolding
    • Raghavan, S. and Kristinsson, H.G. (2007) Conformational and rheological changes in catfish myosin as affected by different acids during acid-induced unfolding and refolding. Journal of Agricultural and Food Chemistry 55: 4144-4153.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , pp. 4144-4153
    • Raghavan, S.1    Kristinsson, H.G.2
  • 107
    • 33746728931 scopus 로고    scopus 로고
    • High hydrostatic pressure and heat treatment effects on physicochemical characteristics of albacore tuna (Thunnus alalunga) minced muscle
    • Ramirez-Suarez, J.C. and Morrissey, M.T. (2006) High hydrostatic pressure and heat treatment effects on physicochemical characteristics of albacore tuna (Thunnus alalunga) minced muscle. Journal of Aquatic Food Product Technology 15: 5-17.
    • (2006) Journal of Aquatic Food Product Technology , vol.15 , pp. 5-17
    • Ramirez-Suarez, J.C.1    Morrissey, M.T.2
  • 108
    • 20444382057 scopus 로고    scopus 로고
    • Antifreeze glycoproteins from the Antarctic fish Dissostichus mawsoni studied by differential scanning calorimetry (DSC) in combination with nanolitre osmometry
    • Ramløv, H., DeVries, A.L. and Wilson, P.W. (2005) Antifreeze glycoproteins from the Antarctic fish Dissostichus mawsoni studied by differential scanning calorimetry (DSC) in combination with nanolitre osmometry. CryoLetters 26: 73-84.
    • (2005) CryoLetters , vol.26 , pp. 73-84
    • Ramløv, H.1    DeVries, A.L.2    Wilson, P.W.3
  • 109
    • 0030758807 scopus 로고    scopus 로고
    • Cryoprotective properties of proline in cod muscle studied by differential scanning calorimetry
    • Rasmussen, P.H., Jørgensen, B. and Nielsen, J. (1997) Cryoprotective properties of proline in cod muscle studied by differential scanning calorimetry. CryoLetters 18: 293-300.
    • (1997) CryoLetters , vol.18 , pp. 293-300
    • Rasmussen, P.H.1    Jørgensen, B.2    Nielsen, J.3
  • 110
    • 84960317998 scopus 로고    scopus 로고
    • Blanchiert oder gegart? - Die Einstufung erhitzter Muscheln (Perna canaliculus) durch Eiwei ßuntersuchung
    • Rehbein, H. and Schubring, R. (1996) Blanchiert oder gegart? - Die Einstufung erhitzter Muscheln (Perna canaliculus) durch Eiwei ßuntersuchung. Informationen für die Fischwirtschaft 43: 29-36.
    • (1996) Informationen für die Fischwirtschaft , vol.43 , pp. 29-36
    • Rehbein, H.1    Schubring, R.2
  • 112
    • 0035706609 scopus 로고    scopus 로고
    • Effect of feed protein levels on digestive proteolytic activity, texture, and thermal denaturation of muscle protein in reared blue shrimp
    • Rivas-Vega, M.E., Rouzaud-Sanchez, O. and Ezquerra-Brauer, J.M. (2001) Effect of feed protein levels on digestive proteolytic activity, texture, and thermal denaturation of muscle protein in reared blue shrimp. Journal of Aquatic Food Product Technology 10: 25-38.
    • (2001) Journal of Aquatic Food Product Technology , vol.10 , pp. 25-38
    • Rivas-Vega, M.E.1    Rouzaud-Sanchez, O.2    Ezquerra-Brauer, J.M.3
  • 113
    • 0011812629 scopus 로고
    • Effect of time, temperature, raw material type, processing and use of cryoprotective agents on mince quality
    • J.J. Connel (Ed), Fishing News Books Ltd, Farnham, Surrey, UK
    • Rodger, G., Weddle, R.B. and Craig, P. (1980) Effect of time, temperature, raw material type, processing and use of cryoprotective agents on mince quality. In: J.J. Connel (Ed) Advances in Fish Science and Technology. Fishing News Books Ltd, Farnham, Surrey, UK, pp. 199-217.
    • (1980) Advances in Fish Science and Technology , pp. 199-217
    • Rodger, G.1    Weddle, R.B.2    Craig, P.3
  • 114
    • 84909654229 scopus 로고
    • Effect of alkaline protease activity on some properties of comminuted squid
    • Rodger, G., Weddle, R.B. and Craig, P., Hastings, R. (1984) Effect of alkaline protease activity on some properties of comminuted squid. Journal of Food Science 49: 117-119, 123.
    • (1984) Journal of Food Science , vol.49
    • Rodger, G.1    Weddle, R.B.2    Craig, P.3    Hastings, R.4
  • 115
    • 29144489235 scopus 로고    scopus 로고
    • Concentration-dependent suppressive effect of shrimp head protein hydrolysate on dehydration-induced denaturation of lizardfish myofibrils
    • Ruttanapornvareesakul, Y., Ikeda, M., Hara, K., Osatomi, K., Osako, K., Kongpun, O. and Nozaki, Y. (2006) Concentration-dependent suppressive effect of shrimp head protein hydrolysate on dehydration-induced denaturation of lizardfish myofibrils. Bioresource Technology 97: 762-769.
    • (2006) Bioresource Technology , vol.97 , pp. 762-769
    • Ruttanapornvareesakul, Y.1    Ikeda, M.2    Hara, K.3    Osatomi, K.4    Osako, K.5    Kongpun, O.6    Nozaki, Y.7
  • 116
    • 0003178635 scopus 로고    scopus 로고
    • Thermal analysis in foods and food processes
    • R.B. Kemp (Ed), Volume IV (From Macromolecules to Man). Elsevier Science B.V., Amsterdam
    • Schiraldi, A., Piazza, L., Fessas, D. and Riva, M. (1999) Thermal analysis in foods and food processes. In: R.B. Kemp (Ed) Handbook of Thermal Analysis and Calorimetry, Volume IV (From Macromolecules to Man). Elsevier Science B.V., Amsterdam, pp. 829-921.
    • (1999) Handbook of Thermal Analysis and Calorimetry , pp. 829-921
    • Schiraldi, A.1    Piazza, L.2    Fessas, D.3    Riva, M.4
  • 117
    • 0039473530 scopus 로고    scopus 로고
    • DSC, TPA, and CIELAB - Tools for quality determination during enzymatic ripening of salted herring
    • J. Luten, T. Börresen and J. Oehlenschläger (Eds), Elsevier, Amsterdam
    • Schubring, R. (1997) DSC, TPA, and CIELAB - Tools for quality determination during enzymatic ripening of salted herring. In: J. Luten, T. Börresen and J. Oehlenschläger (Eds) Seafood from Producer to Consumer, Integrated Approach to Quality. Elsevier, Amsterdam, pp. 331-348.
    • (1997) Seafood from Producer to Consumer, Integrated Approach to Quality , pp. 331-348
    • Schubring, R.1
  • 118
    • 0032595508 scopus 로고    scopus 로고
    • Differential scanning calorimetric investigations on pyloric caeca during ripening of salted herring products
    • Schubring, R. (1999a) Differential scanning calorimetric investigations on pyloric caeca during ripening of salted herring products. Journal of Thermal Analysis and Calorimetry 57: 283-291.
    • (1999) Journal of Thermal Analysis and Calorimetry , vol.57 , pp. 283-291
    • Schubring, R.1
  • 119
    • 0012330851 scopus 로고    scopus 로고
    • DSC studies on deep frozen fishery products
    • Schubring, R. (1999b) DSC studies on deep frozen fishery products. Thermochimica Acta 337: 89-95.
    • (1999) Thermochimica Acta , vol.337 , pp. 89-95
    • Schubring, R.1
  • 120
    • 2342580686 scopus 로고    scopus 로고
    • Differential scanning calorimetric (DSC) measurements on the roe of rainbow trout (Oncorhynchus mykiss): influence of maturation and technological
    • Schubring, R. (2004a) Differential scanning calorimetric (DSC) measurements on the roe of rainbow trout (Oncorhynchus mykiss): influence of maturation and technological. Thermochimica Acta 415: 89-98.
    • (2004) Thermochimica Acta , vol.415 , pp. 89-98
    • Schubring, R.1
  • 121
    • 3242717629 scopus 로고    scopus 로고
    • Instrumental colour, texture, water holding and DSC measurements on frozen cod fillets (Gadus morhua) during long-term storage at different temperatures
    • Schubring, R. (2004b) Instrumental colour, texture, water holding and DSC measurements on frozen cod fillets (Gadus morhua) during long-term storage at different temperatures. Deutsche Lebensmittel-Rundschau 100: 247-254.
    • (2004) Deutsche Lebensmittel-Rundschau , vol.100 , pp. 247-254
    • Schubring, R.1
  • 122
    • 30444457389 scopus 로고    scopus 로고
    • Characterizing protein changes caused by application of high hydrostatic pressure on muscle food by means of DSC
    • Schubring, R. (2005a) Characterizing protein changes caused by application of high hydrostatic pressure on muscle food by means of DSC. Journal of Thermal Analysis and Calorimetry 82: 229-237.
    • (2005) Journal of Thermal Analysis and Calorimetry , vol.82 , pp. 229-237
    • Schubring, R.1
  • 123
    • 28844446294 scopus 로고    scopus 로고
    • Changes in texture, water holding capacity, colour, and thermal stability of frozen cod (Gadus morhua) fillets: effect of frozen storage temperature
    • Schubring, R. (2005b) Changes in texture, water holding capacity, colour, and thermal stability of frozen cod (Gadus morhua) fillets: effect of frozen storage temperature. Deutsche Lebensmittel-Rundschau 101: 484-493.
    • (2005) Deutsche Lebensmittel-Rundschau , vol.101 , pp. 484-493
    • Schubring, R.1
  • 124
    • 33744544494 scopus 로고    scopus 로고
    • Thermal stability, texture, liquid holding capacity and colour of smoked salmon on retail level
    • Schubring, R. (2006a) Thermal stability, texture, liquid holding capacity and colour of smoked salmon on retail level. Thermochimica Acta 445: 168-178.
    • (2006) Thermochimica Acta , vol.445 , pp. 168-178
    • Schubring, R.1
  • 125
    • 84899312188 scopus 로고    scopus 로고
    • Use of 'filtered' smoke and carbon monoxide with fish: a review
    • J.B. Luten, C. Jacobsen, K. Bekaert, A. Saebø and J. Oehlenschläger (Eds), Wageningen Academic Publishers, Wageningen
    • Schubring, R. (2006b) Use of 'filtered' smoke and carbon monoxide with fish: a review. In: J.B. Luten, C. Jacobsen, K. Bekaert, A. Saebø and J. Oehlenschläger (Eds) Seafood Research from Fish to Dish. Quality, Safety and Processing of Wild and Farmed Seafood. Wageningen Academic Publishers, Wageningen, pp. 317-345.
    • (2006) Seafood Research from Fish to Dish. Quality, Safety and Processing of Wild and Farmed Seafood , pp. 317-345
    • Schubring, R.1
  • 126
    • 77951737247 scopus 로고    scopus 로고
    • Veränderungen der Farbe und thermischen Stabilität der Muskelproteine von Räucherforellen während der Kühllagerung
    • Schubring, R. (2006c) Veränderungen der Farbe und thermischen Stabilität der Muskelproteine von Räucherforellen während der Kühllagerung. Informationen aus der Fischereiforschung 53: 52-58.
    • (2006) Informationen aus der Fischereiforschung , vol.53 , pp. 52-58
    • Schubring, R.1
  • 127
    • 34247557422 scopus 로고    scopus 로고
    • DSC measurements on sharks
    • Schubring, R. (2007) DSC measurements on sharks. Thermochimica Acta 458: 124-131.
    • (2007) Thermochimica Acta , vol.458 , pp. 124-131
    • Schubring, R.1
  • 128
    • 33749263564 scopus 로고    scopus 로고
    • Ice storage of fish, new aspects: comparison between flake ice and stream ice - part I: sardine (Sardina pilchardus)
    • Schubring, R. and Meyer, C. (2006a) Ice storage of fish, new aspects: comparison between flake ice and stream ice - part I: sardine (Sardina pilchardus). Deutsche Lebensmittel-Rundschau 102: 405-415.
    • (2006) Deutsche Lebensmittel-Rundschau , vol.102 , pp. 405-415
    • Schubring, R.1    Meyer, C.2
  • 129
    • 33751438739 scopus 로고    scopus 로고
    • Iced storage of fish, new aspects: comparison between flake ice and stream ice - Part II: horse mackerel (Trachurus trachurus)
    • Schubring, R. and Meyer, C. (2006b) Iced storage of fish, new aspects: comparison between flake ice and stream ice - Part II: horse mackerel (Trachurus trachurus). Deutsche Lebensmittel-Rundschau 102: 508-517.
    • (2006) Deutsche Lebensmittel-Rundschau , vol.102 , pp. 508-517
    • Schubring, R.1    Meyer, C.2
  • 130
    • 34249739784 scopus 로고    scopus 로고
    • Iced storage, new aspects: comparison between flake ice and stream ice - part III: herring (Clupea harengus)
    • Schubring, R. and Meyer, C. (2007) Iced storage, new aspects: comparison between flake ice and stream ice - part III: herring (Clupea harengus). Deutsche Lebensmittel-Rundschau 103: 203-212.
    • (2007) Deutsche Lebensmittel-Rundschau , vol.103 , pp. 203-212
    • Schubring, R.1    Meyer, C.2
  • 133
    • 0000071641 scopus 로고
    • Protein interactions in gels: protein-protein interactions
    • N.S. Hettiarachchi and G.R. Ziegler (Eds), Marcel Dekker, New York
    • Smith, D.M. (1994) Protein interactions in gels: protein-protein interactions. In: N.S. Hettiarachchi and G.R. Ziegler (Eds) Protein Functionality in Food Systems. Marcel Dekker, New York, pp. 209-224.
    • (1994) Protein Functionality in Food Systems , pp. 209-224
    • Smith, D.M.1
  • 134
    • 33947663089 scopus 로고    scopus 로고
    • Comparative studies on chemical composition and thermal properties of black tiger shrimp (Penaeus monodon) and white shrimp (Penaeus vannamei) meats
    • Sriket, P., Benjakul, S., Visessanguan, W. and Kijroongrojana, K. (2007) Comparative studies on chemical composition and thermal properties of black tiger shrimp (Penaeus monodon) and white shrimp (Penaeus vannamei) meats. Food Chemistry 103: 1199-1207.
    • (2007) Food Chemistry , vol.103 , pp. 1199-1207
    • Sriket, P.1    Benjakul, S.2    Visessanguan, W.3    Kijroongrojana, K.4
  • 135
    • 0030863688 scopus 로고    scopus 로고
    • Effects of freezing and thawing methods and storage time on thermal properties of freshwater prawns (Macrobrachium rosenbergii)
    • Srinivasan, S., Xiong, Y.L. and Blanchard, S.P. (1997a) Effects of freezing and thawing methods and storage time on thermal properties of freshwater prawns (Macrobrachium rosenbergii). Journal of the Science of Food and Agriculture 75: 37-44.
    • (1997) Journal of the Science of Food and Agriculture , vol.75 , pp. 37-44
    • Srinivasan, S.1    Xiong, Y.L.2    Blanchard, S.P.3
  • 136
    • 0030829476 scopus 로고    scopus 로고
    • Physicochemical changes in prawns (Machrobrachium rosenbergii) subjected to multiple freeze-thaw cycles
    • Srinivasan, S., Xiong, Y.L., Blanchard, S.P. and Tidwell, J.H. (1997b) Physicochemical changes in prawns (Machrobrachium rosenbergii) subjected to multiple freeze-thaw cycles. Journal of Food Science 62: 123-127.
    • (1997) Journal of Food Science , vol.62 , pp. 123-127
    • Srinivasan, S.1    Xiong, Y.L.2    Blanchard, S.P.3    Tidwell, J.H.4
  • 138
    • 0000745165 scopus 로고
    • Physical consequences of thermal reactions in food protein systems
    • H.G. Schwartzberg and R.W. Hartel (Eds), Marcel Dekker, New York
    • Stanley, D.W. and Yada, R.Y. (1992) Physical consequences of thermal reactions in food protein systems. In: H.G. Schwartzberg and R.W. Hartel (Eds) Physical Chemistry of Food. Marcel Dekker, New York, pp. 669-733.
    • (1992) Physical Chemistry of Food , pp. 669-733
    • Stanley, D.W.1    Yada, R.Y.2
  • 139
    • 0000826487 scopus 로고
    • Biochemical applications of differential scanning calorimetry
    • Sturtevant, J.M. (1987) Biochemical applications of differential scanning calorimetry. Annual Review of Physical Chemistry 38: 463-488.
    • (1987) Annual Review of Physical Chemistry , vol.38 , pp. 463-488
    • Sturtevant, J.M.1
  • 140
    • 84987358424 scopus 로고
    • Cryoprotective effects of lactitol, palatinit and polydextrose on cod surimi proteins during frozen storage
    • Sych, J., Lacroix, C., Adambounou, L.T. and Castaigne, F. (1990a) Cryoprotective effects of lactitol, palatinit and polydextrose on cod surimi proteins during frozen storage. Journal of Food Science 55: 356-359.
    • (1990) Journal of Food Science , vol.55 , pp. 356-359
    • Sych, J.1    Lacroix, C.2    Adambounou, L.T.3    Castaigne, F.4
  • 141
    • 84987280162 scopus 로고
    • Cryoprotective effects of some materials on cod surimi proteins during frozen storage
    • Sych, J., Lacroix, C., Adambounou, L.T. and Castaigne, F. (1990b) Cryoprotective effects of some materials on cod surimi proteins during frozen storage. Journal of Food Science 55: 1222-1227, 1263.
    • (1990) Journal of Food Science , vol.55
    • Sych, J.1    Lacroix, C.2    Adambounou, L.T.3    Castaigne, F.4
  • 142
    • 84985278867 scopus 로고
    • Determination of optimal level for lactitol for surimi
    • Sych, J., Lacroix, C. and Carrier, M. (1991a) Determination of optimal level for lactitol for surimi. Journal of Food Science 56: 285-290, 298.
    • (1991) Journal of Food Science , vol.56
    • Sych, J.1    Lacroix, C.2    Carrier, M.3
  • 143
    • 84988119477 scopus 로고
    • The effect of low- or non-sweet additives on the stability of protein functional properties of frozen cod surimi
    • Sych, J., Lacroix, C., Adambounou, L.T. and Castaigne, F. (1991b) The effect of low- or non-sweet additives on the stability of protein functional properties of frozen cod surimi. International Journal of Food Science & Technology 26: 185-197.
    • (1991) International Journal of Food Science & Technology , vol.26 , pp. 185-197
    • Sych, J.1    Lacroix, C.2    Adambounou, L.T.3    Castaigne, F.4
  • 145
    • 33646377204 scopus 로고    scopus 로고
    • Frozen stability of fish protein isolate under various storage conditions
    • Thawornchinsombut, S. and Park, J.W. (2006) Frozen stability of fish protein isolate under various storage conditions. Journal of Food Science 71: C227-C232.
    • (2006) Journal of Food Science , vol.71 , pp. C227-C232
    • Thawornchinsombut, S.1    Park, J.W.2
  • 146
    • 0036097875 scopus 로고    scopus 로고
    • Changes in myofibrillar proteins during processing of salted cod (Gadus morhua) as determined by electrophoresis and differential scanning calorimetry
    • Thorarinsdottir, K.A., Arason, S., Geirsdottir, M., Bogason, S.G. and Kristbergsson, K. (2002) Changes in myofibrillar proteins during processing of salted cod (Gadus morhua) as determined by electrophoresis and differential scanning calorimetry. Food Chemistry 77: 377-385.
    • (2002) Food Chemistry , vol.77 , pp. 377-385
    • Thorarinsdottir, K.A.1    Arason, S.2    Geirsdottir, M.3    Bogason, S.G.4    Kristbergsson, K.5
  • 147
    • 0036265725 scopus 로고    scopus 로고
    • Structural and functional changes in myofibrillar proteins of sea salmon (Pseudopercis semifasciata) by interaction with malonaldehyde (RI)
    • Tironi, V.A., Tomás, M.C. and Añón, M.C. (2002) Structural and functional changes in myofibrillar proteins of sea salmon (Pseudopercis semifasciata) by interaction with malonaldehyde (RI). Journal of Food Science 67: 929-935.
    • (2002) Journal of Food Science , vol.67 , pp. 929-935
    • Tironi, V.A.1    Tomás, M.C.2    Añón, M.C.3
  • 148
    • 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. (2002) Differential scanning calorimetry and circular dichroism spectrometry of walleye pollack myosin and light meromyosin. Journal of Agricultural and Food Chemistry 50: 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
  • 150
    • 7544236251 scopus 로고    scopus 로고
    • Primary structure and thermostability of bigeye tuna myoglobin in relation to those of other scombridae fish
    • Ueki, N. and Ochiai, Y. (2004) Primary structure and thermostability of bigeye tuna myoglobin in relation to those of other scombridae fish. Fisheries Science 70: 875-884.
    • (2004) Fisheries Science , vol.70 , pp. 875-884
    • Ueki, N.1    Ochiai, Y.2
  • 151
    • 21644436544 scopus 로고    scopus 로고
    • Characterization of bullet tuna myoglobin with reference to the thermostability-structure relationship
    • Ueki, N., Chow, C.-J. and Ochiai, Y. (2005) Characterization of bullet tuna myoglobin with reference to the thermostability-structure relationship. Journal of Agricultural and Food Chemistry 53: 4968-4975.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 4968-4975
    • Ueki, N.1    Chow, C.-J.2    Ochiai, Y.3
  • 153
    • 0034091953 scopus 로고    scopus 로고
    • Effects of proteolysis and mechanism of gel weakening in heat-induced gelation of fish myosin
    • Visessanguan, W. and An, H. (2000) Effects of proteolysis and mechanism of gel weakening in heat-induced gelation of fish myosin. Journal of Agricultural and Food Chemistry 48: 1024-1032.
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 1024-1032
    • Visessanguan, W.1    An, H.2
  • 154
    • 0034055958 scopus 로고    scopus 로고
    • Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin
    • Visessanguan, W., Ogawa, M., Nakai, S. and An, H. (2000) Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin. Journal of Agricultural and Food Chemistry 48: 1016-1023.
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 1016-1023
    • Visessanguan, W.1    Ogawa, M.2    Nakai, S.3    An, H.4
  • 155
    • 0031461886 scopus 로고    scopus 로고
    • Carp expresses fast skeletal myosin 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, X.F., Kanoh, S., Chaen, S. and Ooi, T. (1998) Carp expresses fast skeletal myosin isoforms with altered motor functions and structural stabilities to compensate for changes in environmental temperature. Journal of Thermal Biology 22: 375-390.
    • (1998) Journal of Thermal Biology , 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
  • 156
    • 0039163193 scopus 로고
    • Application of scanning calorimetry to the study of protein behaviour in foods
    • B.J.F. Hudson (Ed), Applied Science Publishers, London
    • Wright, D.J. (1982) Application of scanning calorimetry to the study of protein behaviour in foods. In: B.J.F. Hudson (Ed) Developments in Food Proteins - 1. Applied Science Publishers, London, pp. 61-89.
    • (1982) Developments in Food Proteins - 1 , pp. 61-89
    • Wright, D.J.1
  • 157
    • 84985280176 scopus 로고
    • Thermal transitions of admixed starch/fish protein systems during heating
    • Wu, M.C., Lanier, T.C. and Hamann, D.D. (1985) Thermal transitions of admixed starch/fish protein systems during heating. Journal of Food Science 50: 20-25.
    • (1985) Journal of Food Science , vol.50 , pp. 20-25
    • Wu, M.C.1    Lanier, T.C.2    Hamann, D.D.3
  • 158
    • 15744373778 scopus 로고    scopus 로고
    • High-pressure differential scanning calorimetry (DSC): equipment and technique validation using water ice phase-transition data
    • Zhu, S., Bulut, S., Le Bail, A. and Ramaswamy, H.S. (2004) High-pressure differential scanning calorimetry (DSC): equipment and technique validation using water ice phase-transition data. Journal of Food Process Engineering 27: 359-376.
    • (2004) Journal of Food Process Engineering , vol.27 , pp. 359-376
    • Zhu, S.1    Bulut, S.2    Le Bail, A.3    Ramaswamy, H.S.4
  • 159
    • 32844471677 scopus 로고    scopus 로고
    • High-pressure differential scanning calorimetry: Comparison of pressure-dependent phase transition in food materials
    • Zhu, S., Le Bail, A. and Ramaswamy, H.S. (2006a) High-pressure differential scanning calorimetry: Comparison of pressure-dependent phase transition in food materials. Journal of Food Engineering 75: 215-222.
    • (2006) Journal of Food Engineering , vol.75 , pp. 215-222
    • Zhu, S.1    Le Bail, A.2    Ramaswamy, H.S.3
  • 160


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