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Volumn 40, Issue 9, 2007, Pages 1489-1497

Gelling properties of white shrimp (Penaeus vannamei) meat as influenced by setting condition and microbial transglutaminase

Author keywords

Cross linking; Gel; Gelation; MTgase; Penaeus vannamei; Setting; White shrimp

Indexed keywords

CARBOXYLIC ACIDS; ENZYMES; GELS; MICROBIOLOGY; MICROSTRUCTURAL EVOLUTION; POLYMERIZATION;

EID: 34347229772     PISSN: 00236438     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lwt.2006.11.017     Document Type: Article
Times cited : (45)

References (50)
  • 2
    • 0031404812 scopus 로고    scopus 로고
    • Influence of texture of suwari gels on kamaboko gels made from sardine (Sardina poilchardus) surimi
    • Alvarez C., and Tejada M. Influence of texture of suwari gels on kamaboko gels made from sardine (Sardina poilchardus) surimi. Journal of the Science of Food and Agriculture 79 (1997) 472-480
    • (1997) Journal of the Science of Food and Agriculture , vol.79 , pp. 472-480
    • Alvarez, C.1    Tejada, M.2
  • 5
    • 0004202155 scopus 로고    scopus 로고
    • AOAC, Association of Official Analytical Chemists, Washington, DC
    • AOAC. Official methods of analysis. 16th ed (1999), Association of Official Analytical Chemists, Washington, DC
    • (1999) Official methods of analysis. 16th ed
  • 6
    • 0036265727 scopus 로고    scopus 로고
    • Astaxanthin extraction from shrimp waste by lactic fermentation and enzymatic hydrolysis of the carotenoprotein complex
    • Armenta-LÓpez R., Guerrero L.I., and Huerta S. Astaxanthin extraction from shrimp waste by lactic fermentation and enzymatic hydrolysis of the carotenoprotein complex. Journal of Food Science 67 (2002) 1002-1006
    • (2002) Journal of Food Science , vol.67 , pp. 1002-1006
    • Armenta-LÓpez, R.1    Guerrero, L.I.2    Huerta, S.3
  • 7
    • 85008100751 scopus 로고
    • Effect of microbial transglutaminase on the quality of frozen surimi made from various kinds of fish species
    • Asagami T., Ogiwara M., Wakameda A., and Noguchi S. Effect of microbial transglutaminase on the quality of frozen surimi made from various kinds of fish species. Fishery Science 61 (1995) 267-272
    • (1995) Fishery Science , vol.61 , pp. 267-272
    • Asagami, T.1    Ogiwara, M.2    Wakameda, A.3    Noguchi, S.4
  • 8
    • 0038504664 scopus 로고    scopus 로고
    • Effect of medium temperature setting on gelling characteristics of surimi from some tropical fish
    • Benjakul S., Chantarasuwan C., and Visessangaun W. Effect of medium temperature setting on gelling characteristics of surimi from some tropical fish. Food Chemistry 82 (2003) 567-574
    • (2003) Food Chemistry , vol.82 , pp. 567-574
    • Benjakul, S.1    Chantarasuwan, C.2    Visessangaun, W.3
  • 9
    • 0037227661 scopus 로고    scopus 로고
    • Transglutaminase-mediated setting in bigeye snapper surimi
    • Benjakul S., and Visessangaun W. Transglutaminase-mediated setting in bigeye snapper surimi. Food Research International 36 (2003) 253-266
    • (2003) Food Research International , vol.36 , pp. 253-266
    • Benjakul, S.1    Visessangaun, W.2
  • 11
    • 0035665007 scopus 로고    scopus 로고
    • Differences in gelation characteristic of natural actomyosin from two species of bigeye snapper, Priacanthus tayenus and P. macracanthus
    • Benjakul S., Visessanguan W., Ishizaki S., and Tanaka M. Differences in gelation characteristic of natural actomyosin from two species of bigeye snapper, Priacanthus tayenus and P. macracanthus. Journal of Food science 66 (2001) 1311-1318
    • (2001) Journal of Food science , vol.66 , pp. 1311-1318
    • Benjakul, S.1    Visessanguan, W.2    Ishizaki, S.3    Tanaka, M.4
  • 12
    • 0036756466 scopus 로고    scopus 로고
    • Characteristics of muscle from two species of bigeye snapper, Priacanthus tayenus and P. macracanthus
    • Benjakul S., Visessanguan W., and Leelapongwattana K. Characteristics of muscle from two species of bigeye snapper, Priacanthus tayenus and P. macracanthus. Biochemistry 26 (2002) 307-326
    • (2002) Biochemistry , vol.26 , pp. 307-326
    • Benjakul, S.1    Visessanguan, W.2    Leelapongwattana, K.3
  • 13
  • 15
    • 34347239465 scopus 로고
    • A rapid and simple method for the purification of transglutaminase from Streptoverticillium mobaraense
    • Gerber U., Jucknischke U., Putzien S., and Fuchsbauer H.L. A rapid and simple method for the purification of transglutaminase from Streptoverticillium mobaraense. Journal of Biochemistry 229 (1994) 825-829
    • (1994) Journal of Biochemistry , vol.229 , pp. 825-829
    • Gerber, U.1    Jucknischke, U.2    Putzien, S.3    Fuchsbauer, H.L.4
  • 16
    • 0012698485 scopus 로고
    • Viscoelastic properties of surimi seafood products
    • Rao M.A., and Steffe J.F. (Eds), Marcel Dekker, Inc., New York
    • Hamann D.D. Viscoelastic properties of surimi seafood products. In: Rao M.A., and Steffe J.F. (Eds). Viscoelastic properties of foods (1992), Marcel Dekker, Inc., New York 157-171
    • (1992) Viscoelastic properties of foods , pp. 157-171
    • Hamann, D.D.1
  • 17
    • 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. Differential scanning calorimetry of fish muscle: The effect of processing and species variation. Journal of Food Science 50 (1985) 503-510
    • (1985) Journal of Food Science , vol.50 , pp. 503-510
    • Hastings, R.J.1    Rodger, G.W.2    Park, R.3    Matthews, A.D.4    Anderson, E.M.5
  • 18
    • 0034025580 scopus 로고    scopus 로고
    • Technical approach to simplify the purification method and characterization of microbial transglutaminase produced from Streptoverticillium ladakanum
    • Ho M.L., Leu S.Z., Hiseh J.F., and Jiang S.T. Technical approach to simplify the purification method and characterization of microbial transglutaminase produced from Streptoverticillium ladakanum. Journal of Food Science 65 (2000) 76-80
    • (2000) Journal of Food Science , vol.65 , pp. 76-80
    • Ho, M.L.1    Leu, S.Z.2    Hiseh, J.F.3    Jiang, S.T.4
  • 19
    • 0026641632 scopus 로고
    • Cross-linking of contractile proteins from skeletal muscle by treatment with microbial transglutaminase
    • Huang Y.P., Seguro K., Motoki M., and Tawada K. Cross-linking of contractile proteins from skeletal muscle by treatment with microbial transglutaminase. Journal of Biochemistry 112 (1992) 229-234
    • (1992) Journal of Biochemistry , vol.112 , pp. 229-234
    • Huang, Y.P.1    Seguro, K.2    Motoki, M.3    Tawada, K.4
  • 21
    • 0012204094 scopus 로고    scopus 로고
    • Enzymes and their effects on seafood texture
    • Haard N.F., and Simpson B.K. (Eds), Marcel Dekker, Inc, New York
    • Jiang S.T. Enzymes and their effects on seafood texture. In: Haard N.F., and Simpson B.K. (Eds). Seafood enzymes: Utilization and influence on postharvest seafood quality (2000), Marcel Dekker, Inc, New York 411-450
    • (2000) Seafood enzymes: Utilization and influence on postharvest seafood quality , pp. 411-450
    • Jiang, S.T.1
  • 22
    • 0033864267 scopus 로고    scopus 로고
    • Microbial transglutaminase affects gel properties of golden threadfin-bream and Pollack surimi
    • Jiang S.T., Hsieh J.F., Ho M.L., and Chung Y.C. Microbial transglutaminase affects gel properties of golden threadfin-bream and Pollack surimi. Journal of Food Science 65 (2000) 694-699
    • (2000) Journal of Food Science , vol.65 , pp. 694-699
    • Jiang, S.T.1    Hsieh, J.F.2    Ho, M.L.3    Chung, Y.C.4
  • 23
    • 84986522949 scopus 로고
    • Nondisulfide covalent cross-linking of myosin heavy chain in "setting" of Alaska pollock and Atlantic croaker surimi
    • Kamath G.G., Lanier T.C., Foegeding E.A., and Hamann D.D. Nondisulfide covalent cross-linking of myosin heavy chain in "setting" of Alaska pollock and Atlantic croaker surimi. Journal of Food Biochemistry 16 (1992) 151-172
    • (1992) Journal of Food Biochemistry , vol.16 , pp. 151-172
    • Kamath, G.G.1    Lanier, T.C.2    Foegeding, E.A.3    Hamann, D.D.4
  • 25
  • 26
    • 0002836045 scopus 로고
    • Measurement of surimi composition and functional properties
    • Lanier T.C., and Lee C.M. (Eds), Marcel Dekker, Inc, New York
    • Lanier T.C. Measurement of surimi composition and functional properties. In: Lanier T.C., and Lee C.M. (Eds). Surimi technology (1992), Marcel Dekker, Inc, New York 123-166
    • (1992) Surimi technology , pp. 123-166
    • Lanier, T.C.1
  • 27
    • 0013485397 scopus 로고
    • Process innovations in surimi manufacture
    • Lanier T.C., and Lee C.M. (Eds), Marcel Dekker, Inc, New York
    • Lanier T.C., Manning P.K., Zetterling T., and MacDonal G.A. Process innovations in surimi manufacture. In: Lanier T.C., and Lee C.M. (Eds). Surimi technology (1992), Marcel Dekker, Inc, New York 167-179
    • (1992) Surimi technology , pp. 167-179
    • Lanier, T.C.1    Manning, P.K.2    Zetterling, T.3    MacDonal, G.A.4
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structure protein during the assembly of head bacteriophage T4
    • Leammli U.K. Cleavage of structure protein during the assembly of head bacteriophage T4. Nature 277 (1970) 680-685
    • (1970) Nature , vol.277 , pp. 680-685
    • Leammli, U.K.1
  • 30
    • 0034866261 scopus 로고    scopus 로고
    • Surimi of fish species from the gulf of Mexico: Evaluation of the setting phenomenon
    • Morales O.G., Ramirez J.A., Vivanco D.I., and Vazuez D.I. Surimi of fish species from the gulf of Mexico: Evaluation of the setting phenomenon. Food Chemistry 75 (2001) 43-48
    • (2001) Food Chemistry , vol.75 , pp. 43-48
    • Morales, O.G.1    Ramirez, J.A.2    Vivanco, D.I.3    Vazuez, D.I.4
  • 31
    • 84893743812 scopus 로고
    • Protease inhibitor effects on torsion measurements and autolysis of Pacific whiting surimi
    • Morrissey M.T., Wu J.W., Lin D., and An H. Protease inhibitor effects on torsion measurements and autolysis of Pacific whiting surimi. Journal of Food Science 58 (1993) 1054-1059
    • (1993) Journal of Food Science , vol.58 , pp. 1054-1059
    • Morrissey, M.T.1    Wu, J.W.2    Lin, D.3    An, H.4
  • 33
    • 0000404903 scopus 로고    scopus 로고
    • A comparison of cross-linking of fish myofibrillar proteins by endogenous and microbial transglutaminase
    • Nakahara C., Nozawa H., and Seki N. A comparison of cross-linking of fish myofibrillar proteins by endogenous and microbial transglutaminase. Fisheries Science 65 (1999) 138-144
    • (1999) Fisheries Science , vol.65 , pp. 138-144
    • Nakahara, C.1    Nozawa, H.2    Seki, N.3
  • 35
    • 0000323022 scopus 로고
    • Chemistry of surimi gelation
    • Lanier T.C., and Lee C.M. (Eds), Marcel Dekker, Inc, New York
    • Niwa E. Chemistry of surimi gelation. In: Lanier T.C., and Lee C.M. (Eds). Surimi technology (1992), Marcel Dekker, Inc, New York 389-428
    • (1992) Surimi technology , pp. 389-428
    • Niwa, E.1
  • 37
    • 85008062073 scopus 로고    scopus 로고
    • Carotenoid composition in the exoskeleton of commercial black tiger prawns
    • Okada S., Nur-E-Borhan S.A., and Yamaguchi K. Carotenoid composition in the exoskeleton of commercial black tiger prawns. Fishery Science 60 (1998) 213-215
    • (1998) Fishery Science , vol.60 , pp. 213-215
    • Okada, S.1    Nur-E-Borhan, S.A.2    Yamaguchi, K.3
  • 39
    • 84986467761 scopus 로고
    • ε-(γ-glutamyl)lysine crosslink distribution in foods as determined by improved method
    • Sakamoto H., Kumazawa Y., Kawajiri H., and Motoki M. ε-(γ-glutamyl)lysine crosslink distribution in foods as determined by improved method. Journal of Food Science 60 (1995) 416-419
    • (1995) Journal of Food Science , vol.60 , pp. 416-419
    • Sakamoto, H.1    Kumazawa, Y.2    Kawajiri, H.3    Motoki, M.4
  • 40
    • 84986465415 scopus 로고
    • Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture
    • Sakamoto H., Kumazawa Y., Toiguchi S., Seguro K., Soeda T., and Motoki M. Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture. Journal of Food Science 60 (1995) 300-304
    • (1995) Journal of Food Science , vol.60 , pp. 300-304
    • Sakamoto, H.1    Kumazawa, Y.2    Toiguchi, S.3    Seguro, K.4    Soeda, T.5    Motoki, M.6
  • 42
    • 84986446950 scopus 로고
    • Microbial transglutaminase ε-(γ-glutamyl) lysine crosslink effects on elastics properties of kamaboko gels
    • Seguro K., Kumazawa Y., Ohtsuka T., Toiguchi S., and Motoki M. Microbial transglutaminase ε-(γ-glutamyl) lysine crosslink effects on elastics properties of kamaboko gels. Journal of Food Science 60 (1995) 305-311
    • (1995) Journal of Food Science , vol.60 , pp. 305-311
    • Seguro, K.1    Kumazawa, Y.2    Ohtsuka, T.3    Toiguchi, S.4    Motoki, M.5
  • 43
    • 85008134027 scopus 로고
    • Transglutaminase activity in Alaska pollack muscle and surimi, and its reaction with myosin B
    • Seki N., Uno H., Lee N.-H., Kimura I., Toyoda K., Fujita T., et al. Transglutaminase activity in Alaska pollack muscle and surimi, and its reaction with myosin B. Nippon Suisan Gakkaishi 56 (1990) 125-132
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 125-132
    • Seki, N.1    Uno, H.2    Lee, N.-H.3    Kimura, I.4    Toyoda, K.5    Fujita, T.6
  • 44
    • 85004488423 scopus 로고
    • Species variations in the gel forming characteristics of fish meat paste
    • Shimizu Y., Machida R., and Takenemi S. Species variations in the gel forming characteristics of fish meat paste. Nippon Suisan Gakkaishi 47 (1981) 95-104
    • (1981) Nippon Suisan Gakkaishi , vol.47 , pp. 95-104
    • Shimizu, Y.1    Machida, R.2    Takenemi, S.3
  • 45
  • 46
    • 0009278798 scopus 로고
    • Carotenoid pigments in seafood
    • Martin R.E., Flick G.J., and Ward D.R. (Eds), AVI Publishing, Connecticut
    • Simpson K.L. Carotenoid pigments in seafood. In: Martin R.E., Flick G.J., and Ward D.R. (Eds). Chemistry and biochemistry of marine food products (1982), AVI Publishing, Connecticut 115-148
    • (1982) Chemistry and biochemistry of marine food products , pp. 115-148
    • Simpson, K.L.1
  • 48
    • 0001466879 scopus 로고
    • Polymerization and gelation of carp myosin by microbial transglutaminase
    • Tanaka H., Nonaka M., and Motoki M. Polymerization and gelation of carp myosin by microbial transglutaminase. Nippon Suisan Gakkaishi 56 (1990) 1341-1347
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 1341-1347
    • Tanaka, H.1    Nonaka, M.2    Motoki, M.3
  • 49
    • 0030470866 scopus 로고    scopus 로고
    • Transglutaminase from Streptoverticilium ladakanum and application to mince fish product
    • Tsai G.J., Lin S.M., and Jaing S.T. Transglutaminase from Streptoverticilium ladakanum and application to mince fish product. Journal of Food Science 61 (1996) 1234-1238
    • (1996) Journal of Food Science , vol.61 , pp. 1234-1238
    • Tsai, G.J.1    Lin, S.M.2    Jaing, S.T.3
  • 50
    • 85007729648 scopus 로고
    • Molecular cloning of the gene for microbial transglutaminase from Streptoverticillium and its expression in Streptomyces lividans
    • Washizu K., Ando K., Koikeda S., Hirose S., Matsuura A., Takagi H., et al. Molecular cloning of the gene for microbial transglutaminase from Streptoverticillium and its expression in Streptomyces lividans. Bioscience Biotechnology and Biochemistry 58 (1994) 82-87
    • (1994) Bioscience Biotechnology and Biochemistry , vol.58 , pp. 82-87
    • Washizu, K.1    Ando, K.2    Koikeda, S.3    Hirose, S.4    Matsuura, A.5    Takagi, H.6


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