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Volumn , Issue , 2011, Pages 116-149

Seafood proteins

Author keywords

Protein functional properties; Protein recovery; Seafood protein applications; Seafood proteins; Seafood sustainability

Indexed keywords

MARINE BIOLOGY; POPULATION STATISTICS; PROTEINS; RECOVERY; SUSTAINABLE DEVELOPMENT;

EID: 84875457629     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-1-84569-758-7.50006-X     Document Type: Chapter
Times cited : (36)

References (128)
  • 1
    • 0002845599 scopus 로고
    • Fish allergy and the cod fish allergen model
    • Baillière Tindall, London, J. Brostoff, S.J. Challacombe (Eds.)
    • Aas K. Fish allergy and the cod fish allergen model. Food allergy and intolerance 1987, 356-366. Baillière Tindall, London. J. Brostoff, S.J. Challacombe (Eds.).
    • (1987) Food allergy and intolerance , pp. 356-366
    • Aas, K.1
  • 2
    • 0014641848 scopus 로고
    • Characterization of a major allergen (cod): effect of enzymic hydrolysis on the allergenic activity
    • Aas K., Elsayed S. Characterization of a major allergen (cod): effect of enzymic hydrolysis on the allergenic activity. J Allergy 1969, 44:333-343.
    • (1969) J Allergy , vol.44 , pp. 333-343
    • Aas, K.1    Elsayed, S.2
  • 3
    • 0014178556 scopus 로고
    • Studies of hypersensitivity to fish: partial purification and crystallization of a major allergenic component of cod
    • Aas K., Jebsen J.W. Studies of hypersensitivity to fish: partial purification and crystallization of a major allergenic component of cod. Int Arch Allergy Appl Immunol 1967, 32:1-20.
    • (1967) Int Arch Allergy Appl Immunol , vol.32 , pp. 1-20
    • Aas, K.1    Jebsen, J.W.2
  • 6
    • 84985231984 scopus 로고
    • Electrophoretic identification of fish species used in surimi products
    • An A., Wei C., Zhao J., Marshall M., Lee C. Electrophoretic identification of fish species used in surimi products. J Food Sci 1989, 54(2):253-257.
    • (1989) J Food Sci , vol.54 , Issue.2 , pp. 253-257
    • An, A.1    Wei, C.2    Zhao, J.3    Marshall, M.4    Lee, C.5
  • 7
    • 84941307103 scopus 로고    scopus 로고
    • Anonymous [Accessed 27 February 2010]
    • Anonymous [Accessed 27 February 2010]. http://www.dietaryfiberfood.com/protein.
  • 8
    • 0018366389 scopus 로고
    • Characterization of the immunological cross reactivity of fragments TM1 and TM2 of allergen M from cod
    • Apold J., Elsayed S. Characterization of the immunological cross reactivity of fragments TM1 and TM2 of allergen M from cod. Mol Immunol 1979, 16:205-211.
    • (1979) Mol Immunol , vol.16 , pp. 205-211
    • Apold, J.1    Elsayed, S.2
  • 9
    • 0018324838 scopus 로고
    • The effect of amino acid modification and polymerization on the immunochemical reactivity of cod allergen M
    • Apold J., Elsayed S. The effect of amino acid modification and polymerization on the immunochemical reactivity of cod allergen M. Mol Immunol 1979, 16:559-564.
    • (1979) Mol Immunol , vol.16 , pp. 559-564
    • Apold, J.1    Elsayed, S.2
  • 10
    • 0018865920 scopus 로고
    • The immunochemical reactivity of regions encompassing Tyr-30 and Arg-75 of allergen M from cod
    • Apold J., Elsayed S. The immunochemical reactivity of regions encompassing Tyr-30 and Arg-75 of allergen M from cod. Mol Immunol 1980, 17:291-296.
    • (1980) Mol Immunol , vol.17 , pp. 291-296
    • Apold, J.1    Elsayed, S.2
  • 11
    • 0032817784 scopus 로고    scopus 로고
    • High pressure effects on gelation of surimi and turkey breast muscle enhanced by microbial transglutaminase
    • Ashie I.N.A., Lanier T.C. High pressure effects on gelation of surimi and turkey breast muscle enhanced by microbial transglutaminase. J Food Sci 1999, 64:704-708.
    • (1999) J Food Sci , vol.64 , pp. 704-708
    • Ashie, I.N.A.1    Lanier, T.C.2
  • 13
    • 0040585496 scopus 로고    scopus 로고
    • Comparative study of frying to the other cooking techniques. Influence on the nutritive value
    • Bognar A. Comparative study of frying to the other cooking techniques. Influence on the nutritive value. Grasas y Aceites 1998, 49:250-260.
    • (1998) Grasas y Aceites , vol.49 , pp. 250-260
    • Bognar, A.1
  • 14
    • 59949105772 scopus 로고    scopus 로고
    • Edible protein films: properties enhancement - Review article
    • Bourtoom T. Edible protein films: properties enhancement - Review article. Int Food Res J 2009, 16:1-9.
    • (2009) Int Food Res J , vol.16 , pp. 1-9
    • Bourtoom, T.1
  • 18
    • 33749673755 scopus 로고    scopus 로고
    • Quality differences of whole ungutted sea bream (Sparus aurata) and sea bass (Dicentrarchus labrax) while stored in ice
    • Cakli S., Kilinc B., Cadun A., Dincer T., Tolasa S. Quality differences of whole ungutted sea bream (Sparus aurata) and sea bass (Dicentrarchus labrax) while stored in ice. Food Control 2007, 18:391-397.
    • (2007) Food Control , vol.18 , pp. 391-397
    • Cakli, S.1    Kilinc, B.2    Cadun, A.3    Dincer, T.4    Tolasa, S.5
  • 19
    • 33947591849 scopus 로고    scopus 로고
    • Gelation of protein recovered from Antarctic krill (Euphasia superba) by isoelectric solubilization/precipitation as affected by function additives
    • Chen Y.C., Jaczynski J. Gelation of protein recovered from Antarctic krill (Euphasia superba) by isoelectric solubilization/precipitation as affected by function additives. J Agric Food Chem 2007, 55:1814-1822.
    • (2007) J Agric Food Chem , vol.55 , pp. 1814-1822
    • Chen, Y.C.1    Jaczynski, J.2
  • 20
    • 36148946431 scopus 로고    scopus 로고
    • Protein recovery from rainbow trout (Oncorhynchus mykiss) processing by-products via isoelectric solubilization/precipitation
    • Chen Y.C., Jaczynski J. Protein recovery from rainbow trout (Oncorhynchus mykiss) processing by-products via isoelectric solubilization/precipitation. J Agric Food Chem 2007, 55:9079-9088.
    • (2007) J Agric Food Chem , vol.55 , pp. 9079-9088
    • Chen, Y.C.1    Jaczynski, J.2
  • 21
    • 36348996022 scopus 로고    scopus 로고
    • Amino acid, fatty acid, and mineral profiles of materials recovered from rainbow trout (Oncorhynchus my kiss) processing by-products using isoelectric solubilization/precipitation
    • Chen Y.C., Tou J.C., Jaczynski J. Amino acid, fatty acid, and mineral profiles of materials recovered from rainbow trout (Oncorhynchus my kiss) processing by-products using isoelectric solubilization/precipitation. J Food Sci 2007, 72(9):C527-535.
    • (2007) J Food Sci , vol.72 , Issue.9 , pp. C527-535
    • Chen, Y.C.1    Tou, J.C.2    Jaczynski, J.3
  • 22
    • 62549118658 scopus 로고    scopus 로고
    • Amino acid and mineral composition of protein and other components and their recovery from whole Antarctic krill (Euphasia superba) using isoelectric solubilization/precipitation
    • Chen Y.C., Tou J.C., Jaczynski J. Amino acid and mineral composition of protein and other components and their recovery from whole Antarctic krill (Euphasia superba) using isoelectric solubilization/precipitation. J Food Sci 2009, 74(2):H31-H39.
    • (2009) J Food Sci , vol.74 , Issue.2 , pp. H31-H39
    • Chen, Y.C.1    Tou, J.C.2    Jaczynski, J.3
  • 23
    • 0036812288 scopus 로고    scopus 로고
    • Acid-aided protein recovery from enzyme-rich Pacific whiting
    • Choi Y.J., Park J.W. Acid-aided protein recovery from enzyme-rich Pacific whiting. J Food Sci 2002, 67:2962-2967.
    • (2002) J Food Sci , vol.67 , pp. 2962-2967
    • Choi, Y.J.1    Park, J.W.2
  • 24
    • 0026230747 scopus 로고
    • Nutritional, physiological, genetic, sex, and age effects on fat-free dry matter composition of the body in avian, fish, and mammalian species: a review
    • Clawson A.J., Garlich J.D., Coffey M.T., Pon W.G. Nutritional, physiological, genetic, sex, and age effects on fat-free dry matter composition of the body in avian, fish, and mammalian species: a review. J Anim Sci 1991, 69:3617-3644.
    • (1991) J Anim Sci , vol.69 , pp. 3617-3644
    • Clawson, A.J.1    Garlich, J.D.2    Coffey, M.T.3    Pon, W.G.4
  • 26
    • 53649087389 scopus 로고    scopus 로고
    • The effect of steam conditioning practices on pellet quality and growing broiler nutritional value
    • Cutlip S.E., Hott J.M., Buchanan N.P., Rack A.L., Latshaw J.D., Moritz J.S. The effect of steam conditioning practices on pellet quality and growing broiler nutritional value. J Appl Poultry Res 2008, 17:249-261.
    • (2008) J Appl Poultry Res , vol.17 , pp. 249-261
    • Cutlip, S.E.1    Hott, J.M.2    Buchanan, N.P.3    Rack, A.L.4    Latshaw, J.D.5    Moritz, J.S.6
  • 29
    • 0014666651 scopus 로고
    • Freezing resistance in some Antarctic fishes
    • De Vries A.L., Wohlschlag D.E. Freezing resistance in some Antarctic fishes. Science 1969, 163:1074-1075.
    • (1969) Science , vol.163 , pp. 1074-1075
    • De Vries, A.L.1    Wohlschlag, D.E.2
  • 31
    • 3042522694 scopus 로고    scopus 로고
    • Antioxidant activity of flesh and skin of Eptatretus burgeri (Hag fish) and Enedrias nebulosus (White spotted eel)
    • Ekanayake P., Lee Y.D., Lee J. Antioxidant activity of flesh and skin of Eptatretus burgeri (Hag fish) and Enedrias nebulosus (White spotted eel). Food Sci Technol Int 2004, 10:171-177.
    • (2004) Food Sci Technol Int , vol.10 , pp. 171-177
    • Ekanayake, P.1    Lee, Y.D.2    Lee, J.3
  • 32
    • 0015057207 scopus 로고
    • Characterization of a major allergen (cod): observations on effect of denaturation on the allergenic activity
    • Elsayed S., Aas K. Characterization of a major allergen (cod): observations on effect of denaturation on the allergenic activity. J Allergy 1971, 47:283-291.
    • (1971) J Allergy , vol.47 , pp. 283-291
    • Elsayed, S.1    Aas, K.2
  • 33
    • 0020566441 scopus 로고
    • Immunochemical analysis of cod fish allergen M: locations of the immunoglobulin binding sites as demonstrated by the native and synthetic peptides
    • Elsayed S., Apold J. Immunochemical analysis of cod fish allergen M: locations of the immunoglobulin binding sites as demonstrated by the native and synthetic peptides. Allergy 1983, 38:449-459.
    • (1983) Allergy , vol.38 , pp. 449-459
    • Elsayed, S.1    Apold, J.2
  • 34
    • 0015356681 scopus 로고
    • Tryptic cleavage of a homogeneous cod fish allergen and isolation of two active polypeptide fragments
    • Elsayed S., Aas K., Sletten K., Johansson S.G. Tryptic cleavage of a homogeneous cod fish allergen and isolation of two active polypeptide fragments. Immunochemistry 1972, 9:647-661.
    • (1972) Immunochemistry , vol.9 , pp. 647-661
    • Elsayed, S.1    Aas, K.2    Sletten, K.3    Johansson, S.G.4
  • 37
    • 0003651943 scopus 로고
    • FAO Food and Nutrition Papers, No. 51. Rome, Italy
    • FAO/WHO (Food And Agriculture Organizations/World Health Organization) Protein quality evaluation 1990, FAO Food and Nutrition Papers, No. 51. Rome, Italy.
    • (1990) Protein quality evaluation
  • 41
    • 0032997695 scopus 로고    scopus 로고
    • Seaweed proteins: biochemical, nutritional aspects and potential uses
    • Fleurence J. Seaweed proteins: biochemical, nutritional aspects and potential uses. Trends Food Sci Technol 1999, 10:25-28.
    • (1999) Trends Food Sci Technol , vol.10 , pp. 25-28
    • Fleurence, J.1
  • 42
    • 84941307106 scopus 로고    scopus 로고
    • Woodhead Publishing Limited, Cambridge, Proteins in Food Processing
    • Fleurence J. 'Seaweed proteins', in Yada R Y 2004, Woodhead Publishing Limited, Cambridge, Proteins in Food Processing.
    • (2004) 'Seaweed proteins', in Yada R Y
    • Fleurence, J.1
  • 43
    • 2742613660 scopus 로고    scopus 로고
    • Nutritional value of proteins from different food sources - A review
    • Friedman M. Nutritional value of proteins from different food sources - A review. J Agric Food Chem 1996, 44:6-29.
    • (1996) J Agric Food Chem , vol.44 , pp. 6-29
    • Friedman, M.1
  • 44
    • 0346515695 scopus 로고    scopus 로고
    • Isolation and characterization of microorganisms associated with marinated anchovy (Engraulis anchoita)
    • Fuselli S.R., Casales M.R., Fritz R., Yeannes M.I. Isolation and characterization of microorganisms associated with marinated anchovy (Engraulis anchoita). J Aquatic Food Prod Technol 1998, 7:29-38.
    • (1998) J Aquatic Food Prod Technol , vol.7 , pp. 29-38
    • Fuselli, S.R.1    Casales, M.R.2    Fritz, R.3    Yeannes, M.I.4
  • 45
    • 21144479052 scopus 로고
    • Surface activity and related functional properties of peptides obtained from whey protein
    • Gauthier S.F., Paquin P., Pouliot Y., Turgeon S. Surface activity and related functional properties of peptides obtained from whey protein. J Dairy Sci 1993, 76:321-328.
    • (1993) J Dairy Sci , vol.76 , pp. 321-328
    • Gauthier, S.F.1    Paquin, P.2    Pouliot, Y.3    Turgeon, S.4
  • 46
    • 73449140778 scopus 로고    scopus 로고
    • Improvement of pellet quality with proteins recovered from whole fish using isoelectric solubilization/precipitation
    • Gehring C.K., Jaczynski J., Moritz J.S. Improvement of pellet quality with proteins recovered from whole fish using isoelectric solubilization/precipitation. J Appl Poultry Res 2009, 18:418-431.
    • (2009) J Appl Poultry Res , vol.18 , pp. 418-431
    • Gehring, C.K.1    Jaczynski, J.2    Moritz, J.S.3
  • 47
    • 84988097427 scopus 로고
    • Influence of γ-irradiation and ice storage on fat oxidation in three Indian fish
    • Ghadi S.V., Venugopal V. Influence of γ-irradiation and ice storage on fat oxidation in three Indian fish. Int J Food Sci Technol 1991, 26:397-401.
    • (1991) Int J Food Sci Technol , vol.26 , pp. 397-401
    • Ghadi, S.V.1    Venugopal, V.2
  • 49
    • 0001602837 scopus 로고
    • The influence of marination, weight, and cooking technique on tenderness of broilers
    • Goodwin T.L., Maness J.B. The influence of marination, weight, and cooking technique on tenderness of broilers. Poultry Sci 1984, 63:1925-1929.
    • (1984) Poultry Sci , vol.63 , pp. 1925-1929
    • Goodwin, T.L.1    Maness, J.B.2
  • 51
    • 0035804536 scopus 로고    scopus 로고
    • Effect of electric field pulses on microstructure of muscle foods and roes
    • Gudmundsson M., Hafsteinsson H. Effect of electric field pulses on microstructure of muscle foods and roes. Trends Food Sci Technol 2001, 12:122-128.
    • (2001) Trends Food Sci Technol , vol.12 , pp. 122-128
    • Gudmundsson, M.1    Hafsteinsson, H.2
  • 55
    • 69249232042 scopus 로고    scopus 로고
    • Influence of the in vivo addition of alpha-tocopheryl acetate with three lipid sources on the lipid oxidation and fatty acid composition of Beluga sturgeon, Huso huso, during frozen storage
    • Hosseini S.V., Abedian-Kenari A., Rezaei M., Nazari R.M., Feás X., Rabbani M. Influence of the in vivo addition of alpha-tocopheryl acetate with three lipid sources on the lipid oxidation and fatty acid composition of Beluga sturgeon, Huso huso, during frozen storage. Food Chem 2010, 118:341-348.
    • (2010) Food Chem , vol.118 , pp. 341-348
    • Hosseini, S.V.1    Abedian-Kenari, A.2    Rezaei, M.3    Nazari, R.M.4    Feás, X.5    Rabbani, M.6
  • 56
    • 84985258284 scopus 로고    scopus 로고
    • Quality of fish protein hydrolysates from herring (Clupea harengus)
    • Hoyle N.T., Merritt J.H. Quality of fish protein hydrolysates from herring (Clupea harengus). J Food Sci 2003, 59:76-79.
    • (2003) J Food Sci , vol.59 , pp. 76-79
    • Hoyle, N.T.1    Merritt, J.H.2
  • 62
    • 0006070572 scopus 로고    scopus 로고
    • Preparation and characterization of edible films from fish water-soluble proteins
    • Iwata K., Ishizaki S., Handa A., Tanaka M. Preparation and characterization of edible films from fish water-soluble proteins. Fisheries Sci 2000, 66:372-378.
    • (2000) Fisheries Sci , vol.66 , pp. 372-378
    • Iwata, K.1    Ishizaki, S.2    Handa, A.3    Tanaka, M.4
  • 63
    • 0038234765 scopus 로고    scopus 로고
    • Microbial inactivation and electron penetration in surimi seafood during electron beam processing
    • Jaczynski J., Park J.W. Microbial inactivation and electron penetration in surimi seafood during electron beam processing. J Food Sci 2003, 68(5):1788-1792.
    • (2003) J Food Sci , vol.68 , Issue.5 , pp. 1788-1792
    • Jaczynski, J.1    Park, J.W.2
  • 64
    • 0038300742 scopus 로고    scopus 로고
    • Physicochemical properties of surimi seafood as affected by electron beam and heat
    • Jaczynski J., Park J.W. Physicochemical properties of surimi seafood as affected by electron beam and heat. J Food Sci 2003, 68(5):1626-1630.
    • (2003) J Food Sci , vol.68 , Issue.5 , pp. 1626-1630
    • Jaczynski, J.1    Park, J.W.2
  • 65
    • 1242344869 scopus 로고    scopus 로고
    • Physicochemical changes in Alaska pollock surimi and surimi gel as affected by electron beam
    • Jaczynski J., Park J.W. Physicochemical changes in Alaska pollock surimi and surimi gel as affected by electron beam. J Food Sci 2004, 69(1):53-57.
    • (2004) J Food Sci , vol.69 , Issue.1 , pp. 53-57
    • Jaczynski, J.1    Park, J.W.2
  • 66
    • 0017528647 scopus 로고
    • Partial enzymatic hydrolysis of whey protein by trypsin
    • Jost R., Monti J.C., Pahud J.J. Partial enzymatic hydrolysis of whey protein by trypsin. J Dairy Sci 1977, 60:1387-1393.
    • (1977) J Dairy Sci , vol.60 , pp. 1387-1393
    • Jost, R.1    Monti, J.C.2    Pahud, J.J.3
  • 67
    • 0242456060 scopus 로고    scopus 로고
    • Effect of pre-icing duration on quality deterioration of iced Nile perch (Lates niloticus)
    • Karungi C., Byaruhanga Y.B., Muyonga J.H. Effect of pre-icing duration on quality deterioration of iced Nile perch (Lates niloticus). Food Chem 2004, 85:13-17.
    • (2004) Food Chem , vol.85 , pp. 13-17
    • Karungi, C.1    Byaruhanga, Y.B.2    Muyonga, J.H.3
  • 68
  • 69
    • 33646384252 scopus 로고    scopus 로고
    • Functional fish protein ingredients from fish species of warm and temperate waters: comparison of acid- and alkali-aided processing vs. conventional surimi processing
    • P.J. Bechtel (Ed.)
    • Kristinsson H.G., Demir N. Functional fish protein ingredients from fish species of warm and temperate waters: comparison of acid- and alkali-aided processing vs. conventional surimi processing. Advances in Seafood By-products 2003, 277-295. P.J. Bechtel (Ed.).
    • (2003) Advances in Seafood By-products , pp. 277-295
    • Kristinsson, H.G.1    Demir, N.2
  • 70
    • 77349094271 scopus 로고    scopus 로고
    • Fish protein hydrolysates: production, biochemical and functional properties
    • Kristinsson H.G., Rasco B.A. Fish protein hydrolysates: production, biochemical and functional properties. Crit Rev Food Sci Nutr 2000, 32:1-39.
    • (2000) Crit Rev Food Sci Nutr , vol.32 , pp. 1-39
    • Kristinsson, H.G.1    Rasco, B.A.2
  • 71
    • 33748339636 scopus 로고    scopus 로고
    • Surimi gelation chemistry
    • Boca Raton, F, Crc Press (Taylor & Francis Group), J.W. Park (Ed.), 2nd ed.
    • Lanier T.C., Carvajal P., Yongsawatdigul J. Surimi gelation chemistry. Surimi and Surimi Seafood 2005, Boca Raton, F, Crc Press (Taylor & Francis Group). 2nd ed. J.W. Park (Ed.).
    • (2005) Surimi and Surimi Seafood
    • Lanier, T.C.1    Carvajal, P.2    Yongsawatdigul, J.3
  • 72
    • 67650911695 scopus 로고    scopus 로고
    • Survival of Escherichia coli after isoelectric solublization/perciptation of fish
    • Lansdowne L., Beamer S., Jaczynski J., Matak K.E. Survival of Escherichia coli after isoelectric solublization/perciptation of fish. J Food Protect 2009, 72:1398-1403.
    • (2009) J Food Protect , vol.72 , pp. 1398-1403
    • Lansdowne, L.1    Beamer, S.2    Jaczynski, J.3    Matak, K.E.4
  • 73
    • 65549086141 scopus 로고    scopus 로고
    • Survival of Listeria innocua after isoelectric solublization/perciptation of fish protein
    • Lansdowne L., Beamer S., Jaczynski J., Matak K.E. Survival of Listeria innocua after isoelectric solublization/perciptation of fish protein. J Food Sci 2009, 74:M201-M205.
    • (2009) J Food Sci , vol.74 , pp. M201-M205
    • Lansdowne, L.1    Beamer, S.2    Jaczynski, J.3    Matak, K.E.4
  • 75
    • 0016255298 scopus 로고
    • Isolation and characterization of parvalbumins from skeletal muscle of higher vertebrates
    • Lehky P., Blum H.E., Stein E.A., Fisher E.H. Isolation and characterization of parvalbumins from skeletal muscle of higher vertebrates. J Biol Chem 1974, 249:4332-4334.
    • (1974) J Biol Chem , vol.249 , pp. 4332-4334
    • Lehky, P.1    Blum, H.E.2    Stein, E.A.3    Fisher, E.H.4
  • 76
    • 33644984346 scopus 로고    scopus 로고
    • Amino acids composition difference and nutritive evaluation of the muscle of five species of marine fish, Pseudosciaena crocea (large yellow croaker), Lateolabrax japonicus (common sea perch), Pagrosomus major (red seabream), Seriola dumerili (Dumeril's amberjack) and Hapalogenys nitens (black grunt) from Xiamen Bay of China
    • Limin L., Feng X., Jing H. Amino acids composition difference and nutritive evaluation of the muscle of five species of marine fish, Pseudosciaena crocea (large yellow croaker), Lateolabrax japonicus (common sea perch), Pagrosomus major (red seabream), Seriola dumerili (Dumeril's amberjack) and Hapalogenys nitens (black grunt) from Xiamen Bay of China. Aquaculture Nutr 2006, 12:53-59.
    • (2006) Aquaculture Nutr , vol.12 , pp. 53-59
    • Limin, L.1    Feng, X.2    Jing, H.3
  • 77
    • 84920780688 scopus 로고
    • Enzymatic hydrolysis of casein: effect of degree of hydrolysis on antigenicity and physical properties
    • Mahmoud M.I., Malone W.T., Cordle C.T. Enzymatic hydrolysis of casein: effect of degree of hydrolysis on antigenicity and physical properties. J Food Sci 1992, 57:223-229.
    • (1992) J Food Sci , vol.57 , pp. 223-229
    • Mahmoud, M.I.1    Malone, W.T.2    Cordle, C.T.3
  • 78
    • 0035545541 scopus 로고    scopus 로고
    • Assessment of the antioxidant potential of natural food and plant extracts in fresh and previously frozen pork patties
    • Mccarthy T., Kerry J.P., Kerry J.F., Lynch P.B., Buckley D.J. Assessment of the antioxidant potential of natural food and plant extracts in fresh and previously frozen pork patties. Meat Sci 2001, 57:177-184.
    • (2001) Meat Sci , vol.57 , pp. 177-184
    • Mccarthy, T.1    Kerry, J.P.2    Kerry, J.F.3    Lynch, P.B.4    Buckley, D.J.5
  • 79
    • 33746753269 scopus 로고    scopus 로고
    • Functional properties of Rohu (Labeo rohita) proteins during iced storage
    • Mohan M., Ramachandran D., Sankar T.V. Functional properties of Rohu (Labeo rohita) proteins during iced storage. Food Res Int 2006, 39(8):847-854.
    • (2006) Food Res Int , vol.39 , Issue.8 , pp. 847-854
    • Mohan, M.1    Ramachandran, D.2    Sankar, T.V.3
  • 81
    • 0013584013 scopus 로고
    • Difference in amino acid composition of estuarine and marine fucoids
    • Munda I.M. Difference in amino acid composition of estuarine and marine fucoids. Aquatic Botany 1977, 3:273-280.
    • (1977) Aquatic Botany , vol.3 , pp. 273-280
    • Munda, I.M.1
  • 82
    • 0000323022 scopus 로고
    • Chemistry of surimi gelation
    • Marcel Dekker, New York, T.C. Lanier, C.M. Lee (Eds.)
    • Niwa E. Chemistry of surimi gelation. Surimi Technology 1992, Marcel Dekker, New York. T.C. Lanier, C.M. Lee (Eds.).
    • (1992) Surimi Technology
    • Niwa, E.1
  • 83
    • 65149095227 scopus 로고    scopus 로고
    • The acid and alkaline solubilization process for the isolation of muscle proteins: state of the art
    • Nolsoe H., Undeland I. The acid and alkaline solubilization process for the isolation of muscle proteins: state of the art. J Food Bioprocess Technol 2009, 2:1-27.
    • (2009) J Food Bioprocess Technol , vol.2 , pp. 1-27
    • Nolsoe, H.1    Undeland, I.2
  • 84
    • 0002462262 scopus 로고    scopus 로고
    • Protein dispersions and hydrolysates from shark (Isurus oxyrinchus)
    • Onodenalore A.C., Shahidi F. Protein dispersions and hydrolysates from shark (Isurus oxyrinchus). J Aquat Food Prod Technol 1998, 5:43-59.
    • (1998) J Aquat Food Prod Technol , vol.5 , pp. 43-59
    • Onodenalore, A.C.1    Shahidi, F.2
  • 85
    • 0001258048 scopus 로고
    • Heat-induced changes in sulfhydryl groups and disulfide bonds in fish protein and their effect on protein and amino acid digestibility in rainbow trout (Salmo gairneri)
    • Opstvedt J., Miller R., Hardy R.W., Spinelli J. Heat-induced changes in sulfhydryl groups and disulfide bonds in fish protein and their effect on protein and amino acid digestibility in rainbow trout (Salmo gairneri). J Agric Food Chem 1984, 32:929-935.
    • (1984) J Agric Food Chem , vol.32 , pp. 929-935
    • Opstvedt, J.1    Miller, R.2    Hardy, R.W.3    Spinelli, J.4
  • 86
    • 32244449031 scopus 로고    scopus 로고
    • Amino acid and fatty acid composition of wild sea bass (Dicentrarchus labrax): a seasonal differentiation
    • Özyurt G., Polat A. Amino acid and fatty acid composition of wild sea bass (Dicentrarchus labrax): a seasonal differentiation. Eur Food Res Technol 2006, 222:316-320.
    • (2006) Eur Food Res Technol , vol.222 , pp. 316-320
    • Özyurt, G.1    Polat, A.2
  • 87
    • 58849129014 scopus 로고    scopus 로고
    • Sensory, microbiological and chemical assessment of the freshness of red mullet (Mullus barbatus) and goldband goatfish (Upeneus moluccensis) during storage in ice
    • Özyurt G., Kuley E., Özkütük S., Özogul F. Sensory, microbiological and chemical assessment of the freshness of red mullet (Mullus barbatus) and goldband goatfish (Upeneus moluccensis) during storage in ice. Food Chem 2009, 114:505-510.
    • (2009) Food Chem , vol.114 , pp. 505-510
    • Özyurt, G.1    Kuley, E.2    Özkütük, S.3    Özogul, F.4
  • 88
    • 0342700234 scopus 로고    scopus 로고
    • Postmortem biochemical and functional characteristic of Monterey sardine muscle stored at 0°C
    • Pacheco-Aguilar R., Lugo-Sánchez M.E., Robles-Burgueño M.R. Postmortem biochemical and functional characteristic of Monterey sardine muscle stored at 0°C. J Food Sci 2000, 65:40-47.
    • (2000) J Food Sci , vol.65 , pp. 40-47
    • Pacheco-Aguilar, R.1    Lugo-Sánchez, M.E.2    Robles-Burgueño, M.R.3
  • 91
    • 33847014658 scopus 로고    scopus 로고
    • Irradiation preservation of foods
    • Marcel Dekker, New York, M.S. Rahman (Ed.)
    • Rahman M.S. Irradiation preservation of foods. Handbook of Food Preservation 1999, Marcel Dekker, New York. M.S. Rahman (Ed.).
    • (1999) Handbook of Food Preservation
    • Rahman, M.S.1
  • 93
    • 0036218461 scopus 로고    scopus 로고
    • Effect of lipid oxidation and frozen storage on muscle proteins of Atlantic mackerel (Scomber scombrus)
    • Saeed S., Howell N. Effect of lipid oxidation and frozen storage on muscle proteins of Atlantic mackerel (Scomber scombrus). J Sci Food Agric 2002, 82:579-586.
    • (2002) J Sci Food Agric , vol.82 , pp. 579-586
    • Saeed, S.1    Howell, N.2
  • 94
    • 33746870011 scopus 로고    scopus 로고
    • Effect of grape antioxidant dietary fiber on the prevention of lipid oxidation in minced fish: Evaluation by different methodologies
    • Sánchez-Alonso I., Jiménez-Escrig A., Saura-Calixto F., Borderías A.J. Effect of grape antioxidant dietary fiber on the prevention of lipid oxidation in minced fish: Evaluation by different methodologies. Food Chem 2007, 101:372-378.
    • (2007) Food Chem , vol.101 , pp. 372-378
    • Sánchez-Alonso, I.1    Jiménez-Escrig, A.2    Saura-Calixto, F.3    Borderías, A.J.4
  • 95
    • 84971620957 scopus 로고
    • Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation
    • Sano T., Noguchi S.F., Tsuchiya T., Matsumoto J.J. Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation. J Food Sci 1988, 53:924-928.
    • (1988) J Food Sci , vol.53 , pp. 924-928
    • Sano, T.1    Noguchi, S.F.2    Tsuchiya, T.3    Matsumoto, J.J.4
  • 97
    • 3843137481 scopus 로고    scopus 로고
    • Properties of protein powders from arrowtooth flounder (Atheresthes stomias) and herring (Clupea harengus) by-product
    • Sathivel S., Bechtel P.J., Babbitt J., Prinyawiwatkul W., Negulescu I.I., Reppond K.D. Properties of protein powders from arrowtooth flounder (Atheresthes stomias) and herring (Clupea harengus) by-product. J Agric Food Chem 2004, 52:5040-5046.
    • (2004) J Agric Food Chem , vol.52 , pp. 5040-5046
    • Sathivel, S.1    Bechtel, P.J.2    Babbitt, J.3    Prinyawiwatkul, W.4    Negulescu, I.I.5    Reppond, K.D.6
  • 99
    • 0032004375 scopus 로고    scopus 로고
    • Studies on the methionine requirement of carp (Cyprinus carpio L.)
    • Schwarz F.J., Kirchgessner M., Deuringer U. Studies on the methionine requirement of carp (Cyprinus carpio L.). Aquaculture 1998, 161:121-129.
    • (1998) Aquaculture , vol.161 , pp. 121-129
    • Schwarz, F.J.1    Kirchgessner, M.2    Deuringer, U.3
  • 102
    • 0035746634 scopus 로고    scopus 로고
    • Enzymes from fish and aquatic invertebrates and their application in the food industry
    • Shahidi F., Kamil Y.V.A.J. Enzymes from fish and aquatic invertebrates and their application in the food industry. Trends Food Sci Technol 2001, 12:435-464.
    • (2001) Trends Food Sci Technol , vol.12 , pp. 435-464
    • Shahidi, F.1    Kamil, Y.V.A.J.2
  • 103
    • 0029029764 scopus 로고
    • Production and characteristics of protein hydrolysates from capelin (Mallotus villosus)
    • Shahidi F., Han X.-Q., Synowiecki J. Production and characteristics of protein hydrolysates from capelin (Mallotus villosus). Food Chem 1995, 53:285-293.
    • (1995) Food Chem , vol.53 , pp. 285-293
    • Shahidi, F.1    Han, X.-Q.2    Synowiecki, J.3
  • 104
    • 0000665651 scopus 로고
    • Theories of protein denaturation during frozen storage of fish flesh
    • Shenouda S.Y.K. Theories of protein denaturation during frozen storage of fish flesh. Adv Food Res 1980, 26:275-311.
    • (1980) Adv Food Res , vol.26 , pp. 275-311
    • Shenouda, S.Y.K.1
  • 105
    • 0003103547 scopus 로고
    • Changes in protein in frozen stored fish
    • Chapman and Hal, New York, Z. Sikorski, B. Sun Pan, F. Shahidi (Eds.)
    • Sikorski Z., Kolakowska A. Changes in protein in frozen stored fish. Seafood Proteins 1994, Chapman and Hal, New York. Z. Sikorski, B. Sun Pan, F. Shahidi (Eds.).
    • (1994) Seafood Proteins
    • Sikorski, Z.1    Kolakowska, A.2
  • 107
    • 79952607452 scopus 로고    scopus 로고
    • Composition of marine and freshwater finfish and shellfish species and their products
    • Technomic Publishing Company, Lancaster, PA, R.E. Martin, E.P. Carter, G.I. Flick-Jr, L.M. Davis (Eds.)
    • Silva J.L., Chamul R.S. Composition of marine and freshwater finfish and shellfish species and their products. Marine and Freshwater Products Handbook 2000, Technomic Publishing Company, Lancaster, PA. R.E. Martin, E.P. Carter, G.I. Flick-Jr, L.M. Davis (Eds.).
    • (2000) Marine and Freshwater Products Handbook
    • Silva, J.L.1    Chamul, R.S.2
  • 108
    • 0031200776 scopus 로고    scopus 로고
    • Quality assessment of seven Mediterranean fish species during storage on ice
    • Simeonidou S., Govaris A., Vareltzis K. Quality assessment of seven Mediterranean fish species during storage on ice. Food Res Int 1997, 30(7):479-484.
    • (1997) Food Res Int , vol.30 , Issue.7 , pp. 479-484
    • Simeonidou, S.1    Govaris, A.2    Vareltzis, K.3
  • 111
    • 0035037433 scopus 로고    scopus 로고
    • Influence of plasticizers on the properties of edible films prepared from fish water-soluble proteins
    • Tanaka M., Iwata K., Sanguandeekul R., Handa A., Ishizaki S. Influence of plasticizers on the properties of edible films prepared from fish water-soluble proteins. Fisheries Sci 2001, 67:346-351.
    • (2001) Fisheries Sci , vol.67 , pp. 346-351
    • Tanaka, M.1    Iwata, K.2    Sanguandeekul, R.3    Handa, A.4    Ishizaki, S.5
  • 112
    • 62449217825 scopus 로고    scopus 로고
    • Functional properties of proteins recovered from whole gutted silver carp (Hypophthalmichthys molitrix) by isoelecteric solubilization/precipitation
    • Taskaya L., Chen Y.C., Jaczynski J. Functional properties of proteins recovered from whole gutted silver carp (Hypophthalmichthys molitrix) by isoelecteric solubilization/precipitation. LWT - Food Sci Technol 2009, 46(2):1082-1089.
    • (2009) LWT - Food Sci Technol , vol.46 , Issue.2 , pp. 1082-1089
    • Taskaya, L.1    Chen, Y.C.2    Jaczynski, J.3
  • 113
    • 59349088005 scopus 로고    scopus 로고
    • Texture and color properties of proteins recovered from whole gutted silver carp (Hypophthalmichthys molitrix) using isoelecteric solubilization/precipitation
    • Taskaya L., Chen Y.C., Beamer S., Jaczynski J. Texture and color properties of proteins recovered from whole gutted silver carp (Hypophthalmichthys molitrix) using isoelecteric solubilization/precipitation. J Sci Food Agric 2009, 89(2):349-358.
    • (2009) J Sci Food Agric , vol.89 , Issue.2 , pp. 349-358
    • Taskaya, L.1    Chen, Y.C.2    Beamer, S.3    Jaczynski, J.4
  • 114
    • 66149171648 scopus 로고    scopus 로고
    • Compositional characteristics of materials recovered from whole gutted silver carp (Hypophthalmichthys molitrix) using isoelectric solubilization/precipitation
    • Taskaya L., Chen Y.C., Beamer S., Tou J.C., Jaczynski J. Compositional characteristics of materials recovered from whole gutted silver carp (Hypophthalmichthys molitrix) using isoelectric solubilization/precipitation. J Agric Food Chem 2009, 57(10):4259-4266.
    • (2009) J Agric Food Chem , vol.57 , Issue.10 , pp. 4259-4266
    • Taskaya, L.1    Chen, Y.C.2    Beamer, S.3    Tou, J.C.4    Jaczynski, J.5
  • 116
    • 84985201011 scopus 로고
    • Salt induced, low-temperature setting of Antarctic fish muscle proteins
    • Torley P.J., Ingram J., Young O.A., Meyer-Rochow V.B. Salt induced, low-temperature setting of Antarctic fish muscle proteins. J Food Sci 1991, 56:251-252.
    • (1991) J Food Sci , vol.56 , pp. 251-252
    • Torley, P.J.1    Ingram, J.2    Young, O.A.3    Meyer-Rochow, V.B.4
  • 118
    • 33947546891 scopus 로고    scopus 로고
    • Krill for human consumption: nutritional value and potential health benefits
    • Tou J.C., Jaczynski J., Chen Y.C. Krill for human consumption: nutritional value and potential health benefits. Nutr Rev 2007, 65(2):63-77.
    • (2007) Nutr Rev , vol.65 , Issue.2 , pp. 63-77
    • Tou, J.C.1    Jaczynski, J.2    Chen, Y.C.3
  • 119
    • 50349101810 scopus 로고    scopus 로고
    • Effects of cooking methods on the proximate composition and fatty acid composition of seabass (Dicentrarchus labrax, Linnaeus, 1758)
    • Türkkan A.U., Cakli S., Kilinc B. Effects of cooking methods on the proximate composition and fatty acid composition of seabass (Dicentrarchus labrax, Linnaeus, 1758). Food Bioproducts Processing 2008, 86:163-166.
    • (2008) Food Bioproducts Processing , vol.86 , pp. 163-166
    • Türkkan, A.U.1    Cakli, S.2    Kilinc, B.3
  • 120
    • 0037021586 scopus 로고    scopus 로고
    • Recovery of functional proteins from herring (Clupea harengus) light muscle by an acid or alkali solubilization process
    • Undeland I., Kelleher S., Hultin H.O. Recovery of functional proteins from herring (Clupea harengus) light muscle by an acid or alkali solubilization process. J Agric Food Chem 2002, 50:7371-7379.
    • (2002) J Agric Food Chem , vol.50 , pp. 7371-7379
    • Undeland, I.1    Kelleher, S.2    Hultin, H.O.3
  • 121
    • 0343371674 scopus 로고    scopus 로고
    • The determination of flesh productivity and protein components of some fish species after hot smoking
    • Ünlüsain M., Kaleli S., Gulyavuz H. The determination of flesh productivity and protein components of some fish species after hot smoking. J Sci Food Agric 2001, 81(7):661-664.
    • (2001) J Sci Food Agric , vol.81 , Issue.7 , pp. 661-664
    • Ünlüsain, M.1    Kaleli, S.2    Gulyavuz, H.3
  • 125
    • 0032416872 scopus 로고    scopus 로고
    • Viscosity and stability of structural proteins of irradiated Indian mackerel
    • Venugopal V., Doke S.N., Thomas P. Viscosity and stability of structural proteins of irradiated Indian mackerel. J Food Sci 1998, 63(4):648-651.
    • (1998) J Food Sci , vol.63 , Issue.4 , pp. 648-651
    • Venugopal, V.1    Doke, S.N.2    Thomas, P.3
  • 127
    • 0017498915 scopus 로고
    • Differential scanning calorimetric studies of muscle and its constituent proteins
    • Wright D.J., Leach I.B., Wilding P. Differential scanning calorimetric studies of muscle and its constituent proteins. J Sci Food Agr 1977, 28(6):557-564.
    • (1977) J Sci Food Agr , vol.28 , Issue.6 , pp. 557-564
    • Wright, D.J.1    Leach, I.B.2    Wilding, P.3
  • 128
    • 29044432692 scopus 로고    scopus 로고
    • Marination of sheep muscles under pressure and its effect on meat texture quality
    • Yashoda K.P., Rao R.J., Mahendrakar N.S., Rao D.N. Marination of sheep muscles under pressure and its effect on meat texture quality. J Muscle Foods 2005, 16:184-191.
    • (2005) J Muscle Foods , vol.16 , pp. 184-191
    • Yashoda, K.P.1    Rao, R.J.2    Mahendrakar, N.S.3    Rao, D.N.4


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