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Volumn 45, Issue 1, 2010, Pages 48-55

Effect of protein additives, sodium ascorbate, and microbial transglutaminase on the texture and colour of red tilapia surimi gel

Author keywords

Beef plasma protein; Egg white; Microbial transglutaminase; Protein additive; Red tilapia; Sodium ascorbate; Surimi; Tilapia

Indexed keywords

OREOCHROMIS; TILAPIA;

EID: 72449141775     PISSN: 09505423     EISSN: 13652621     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2009.02102.x     Document Type: Article
Times cited : (70)

References (38)
  • 2
    • 0038504664 scopus 로고    scopus 로고
    • Effect of medium temperature setting on gelling characteristics of surimi from some tropical fish
    • Benjakul, S., Chantarasuwan, C. Visessanguan, W. (2003). Effect of medium temperature setting on gelling characteristics of surimi from some tropical fish. Food Chemistry, 82, 567 574.
    • (2003) Food Chemistry , vol.82 , pp. 567-574
    • Benjakul, S.1    Chantarasuwan, C.2    Visessanguan, W.3
  • 4
    • 0036194585 scopus 로고    scopus 로고
    • Thermogelation in plasma protein-added surimi of horse mackerel and the changes in its physical characteristics in stewed products
    • Chen, H.-H. (2002). Thermogelation in plasma protein-added surimi of horse mackerel and the changes in its physical characteristics in stewed products. Fisheries Science, 68, 190 196.
    • (2002) Fisheries Science , vol.68 , pp. 190-196
    • Chen, H.-H.1
  • 5
    • 0004236701 scopus 로고
    • 2nd edn. New York. John Wiley and Sons.
    • Cochran, W. C. Cox, G. M. (1992). Experimental Design, 2nd edn. Pp. 95 145. New York : John Wiley and Sons.
    • (1992) Experimental Design , pp. 95-145
    • Cochran, W.C.1    Cox, G.M.2
  • 6
    • 0008661628 scopus 로고
    • Interaction of myosin-albumin and myosin-fibrinogen to form protein gels
    • Foegeding, E. A., Dayton, W. R. Allen, C. E. (1986). Interaction of myosin-albumin and myosin-fibrinogen to form protein gels. Journal of Food Science, 51, 109 112.
    • (1986) Journal of Food Science , vol.51 , pp. 109-112
    • Foegeding, E.A.1    Dayton, W.R.2    Allen, C.E.3
  • 7
    • 84987350929 scopus 로고
    • Inhibition of modori (gel weakening) in surimi by plasma hydrolysate and egg white
    • Hamann, D. D., Amato, P. M., Wu, M. C. Foegeding, E.A. (1990). Inhibition of modori (gel weakening) in surimi by plasma hydrolysate and egg white. Journal of Food Science, 55, 665 669.
    • (1990) Journal of Food Science , vol.55 , pp. 665-669
    • Hamann, D.D.1    Amato, P.M.2    Wu, M.C.3    Foegeding, E.A.4
  • 8
    • 51749125660 scopus 로고    scopus 로고
    • Thermal stability of fish natural actomyosin affected reactivity to cross-linking by microbial and fish transglutaminases
    • Hemung, B., Li-Chan, E. C. Y. Yongsawatdigul, J. (2008). Thermal stability of fish natural actomyosin affected reactivity to cross-linking by microbial and fish transglutaminases. Food Chemistry, 111, 439 446.
    • (2008) Food Chemistry , vol.111 , pp. 439-446
    • Hemung, B.1    Li-Chan, E.C.Y.2    Yongsawatdigul, J.3
  • 9
    • 0036812824 scopus 로고    scopus 로고
    • Microbial transglutaminase and recombinant cystatin effects on improving the quality of mackerel surimi
    • Hsieh, J.-F., Tsai, G.-F. Jiang, S.-T. (2002). Microbial transglutaminase and recombinant cystatin effects on improving the quality of mackerel surimi. Journal of Food Science, 67, 3120 3125.
    • (2002) Journal of Food Science , vol.67 , pp. 3120-3125
    • Hsieh, J.-F.1    Tsai, G.-F.2    Jiang, S.-T.3
  • 10
    • 0036243442 scopus 로고    scopus 로고
    • Effects of water, oil, starch, calcium carbonate and titanium dioxide on the colour and texture of threadfin and hairtail surimi gels
    • Hsu, C. K. Chiang, B. H. (2002). Effects of water, oil, starch, calcium carbonate and titanium dioxide on the colour and texture of threadfin and hairtail surimi gels. International Journal of Food Science and Technology, 37, 387 393.
    • (2002) International Journal of Food Science and Technology , vol.37 , pp. 387-393
    • Hsu, C.K.1    Chiang, B.H.2
  • 11
    • 0032282398 scopus 로고    scopus 로고
    • Suitability of hybrid tilapia (Oreochromis niloicus x Oreochromis aureus) muscle for gel formation
    • Huang, C.-H., Lai, H.-T. Weng, Y.-M. (1998). Suitability of hybrid tilapia (Oreochromis niloicus x Oreochromis aureus) muscle for gel formation. International Journal of Food Science and Technology, 33, 339 344.
    • (1998) International Journal of Food Science and Technology , vol.33 , pp. 339-344
    • Huang, C.-H.1    Lai, H.-T.2    Weng, Y.-M.3
  • 12
    • 0033864267 scopus 로고    scopus 로고
    • Microbial transglutaminase affects gel properties of golden threadfin-bream and Pollock surimi
    • Jiang, S.-T., Hsieh, J.-F, Ho, M.-L. Chung, Y.-C. (2000). Microbial transglutaminase affects gel properties of golden threadfin-bream and Pollock surimi. Journal of Food Science, 65, 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
  • 13
    • 0032743947 scopus 로고    scopus 로고
    • Bovine plasma protein functions in surimi gelation compared with cysteine protease inhibitors
    • Kang, I. S. Lanier, T. C. (1999). Bovine plasma protein functions in surimi gelation compared with cysteine protease inhibitors. Journal of Food Science, 64, 842 846.
    • (1999) Journal of Food Science , vol.64 , pp. 842-846
    • Kang, I.S.1    Lanier, T.C.2
  • 14
    • 26844557071 scopus 로고    scopus 로고
    • Physical behavior of tilapia surimi gels at various thermal treatment as compared with Alaska Pollack and Pacific whiting surimi
    • Klesk, K., Yongsawatdigul, J., Park, J. W., Viratchakul, S. Virulhakul, P. (2000). Physical behavior of tilapia surimi gels at various thermal treatment as compared with Alaska Pollack and Pacific whiting surimi. Journal of Aquatic Food Product Technology, 9, 91 104.
    • (2000) Journal of Aquatic Food Product Technology , vol.9 , pp. 91-104
    • Klesk, K.1    Yongsawatdigul, J.2    Park, J.W.3    Viratchakul, S.4    Virulhakul, P.5
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T 4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T 4. Nature, 227, 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0001554239 scopus 로고    scopus 로고
    • Gelation chemistry
    • (edited by J.W. Park). New York: Marcel Dekker Inc.
    • Lanier, T.C. (2000). Gelation chemistry. In : Surimi and Surimi Seafood (edited by J.W. Park). Pp. 237 265. New York : Marcel Dekker Inc.
    • (2000) Surimi and Surimi Seafood , pp. 237-265
    • Lanier, T.C.1
  • 17
    • 0000645205 scopus 로고
    • Ingredient and formulation technology for surimi-based products
    • (edited by T.C. Lanier C.M. Lee). New York : Marcel Dekker Inc.
    • Lee, C.M., Wu, M. Okada, M. (1992a). Ingredient and formulation technology for surimi-based products. In : Surimi Technology (edited by T.C. Lanier C.M. Lee). Pp. 273 302. New York : Marcel Dekker Inc.
    • (1992) Surimi Technology , pp. 273-302
    • Lee, C.M.1    Wu, M.2    Okada, M.3
  • 18
  • 19
    • 0030803491 scopus 로고    scopus 로고
    • Transglutaminase effects on low temperature gelation of fish protein sols
    • Lee, H.G., Lanier, T.C., Hamann, D.D. Knopp, J.A. (1997). Transglutaminase effects on low temperature gelation of fish protein sols. Journal of Food Science, 62, 20 24.
    • (1997) Journal of Food Science , vol.62 , pp. 20-24
    • Lee, H.G.1    Lanier, T.C.2    Hamann, D.D.3    Knopp, J.A.4
  • 21
    • 84893743812 scopus 로고
    • Protease inhibitor effects on torsion measurements and autolysis of Pacific whiting surimi
    • Morrissey, M.T., Wu, J.W. An, H. (1993). Protease inhibitor effects on torsion measurements and autolysis of Pacific whiting surimi. Journal of Food Science, 58, 1050 1054.
    • (1993) Journal of Food Science , vol.58 , pp. 1050-1054
    • Morrissey, M.T.1    Wu, J.W.2    An, H.3
  • 22
    • 72449121333 scopus 로고
    • National Fisheries Institute. (edited by T.C. Lanier, K. Hart R.E. Martin). Washington, DC: National Fisheries Institute
    • National Fisheries Institute 1991). A Manual of Standard Methods for Measuring and Specifying the Properties of Surimi (edited by T.C. Lanier, K. Hart R.E. Martin). Pp. 26. Washington, DC : National Fisheries Institute.
    • (1991) A Manual of Standard Methods for Measuring and Specifying the Properties of Surimi , pp. 26
  • 23
    • 0003142124 scopus 로고
    • Measurement of free and expressible drips
    • (edited by H. Hasegawa). Singapore: Asian Fisheries Development Center
    • Ng, C.S. (1987). Measurement of free and expressible drips. In : Laboratory Manual on analytical Methods and Procedure for Fish and Fish Products (edited by H. Hasegawa). Pp. 1 2. Singapore : Asian Fisheries Development Center.
    • (1987) Laboratory Manual on Analytical Methods and Procedure for Fish and Fish Products , pp. 1-2
    • Ng, C.S.1
  • 24
    • 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
  • 25
    • 0000550613 scopus 로고    scopus 로고
    • Ingredient technology and formulation development
    • (edited by J.W. Park). New York: Marcel Dekker Inc.
    • Park, J.W. (2000). Ingredient technology and formulation development. In : Surimi and Surimi Seafood (edited by J.W. Park). Pp. 343 392. New York : Marcel Dekker Inc.
    • (2000) Surimi and Surimi Seafood , pp. 343-392
    • Park, J.W.1
  • 26
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson, G.L. (1977). A simplification of the protein assay method of Lowry et al. which is more generally applicable. Analytical Biochemistry, 83, 346 356.
    • (1977) Analytical Biochemistry , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 27
    • 0036320050 scopus 로고    scopus 로고
    • Using salt and microbial transglutaminase as binding agents in restructured fish products resembling hams
    • Ramirez, J.A., Uresti, R., Tellez, S. Vazquez, M. (2002). Using salt and microbial transglutaminase as binding agent in restructure fish products resembling hams. Journal of Food Science, 67, 1778 1784. (Pubitemid 34817092)
    • (2002) Journal of Food Science , vol.67 , Issue.5 , pp. 1778-1784
    • Ramirez, J.1    Uresti, R.2    Tellez, S.3    Vazquez, M.4
  • 29
    • 33845257852 scopus 로고    scopus 로고
    • Low-salt restructured products from striped mullet (Mugil cephalus) using microbial transglutaminase or whey protein concentrate as additives
    • Ramirez, J.A., del Angel, A., Uresti, R.M., Velazquez, G. Vazquez, M. (2007b). Low-salt restructured products from striped mullet (Mugil cephalus) using microbial transglutaminase or whey protein concentrate as additives. Food Chemistry, 102, 243 249.
    • (2007) Food Chemistry , vol.102 , pp. 243-249
    • Ramirez, J.A.1    Del Angel, A.2    Uresti, R.M.3    Velazquez, G.4    Vazquez, M.5
  • 30
    • 34547335233 scopus 로고    scopus 로고
    • Effect of chicken plasma protein and some protein additives on proteolysis and gel-forming ability of sardine (Sardinella gibbosa) surimi
    • Rawdkuen, S., Benjakul, S., Visessanguan, W. Lanier, T.C. (2007). Effect of chicken plasma protein and some protein additives on proteolysis and gel-forming ability of sardine (Sardinella gibbosa) surimi. Journal of Food Processing and Preservation, 31, 492 516.
    • (2007) Journal of Food Processing and Preservation , vol.31 , pp. 492-516
    • Rawdkuen, S.1    Benjakul, S.2    Visessanguan, W.3    Lanier, T.C.4
  • 31
    • 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. Motoki, M. (1995). Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture. Journal of Food Science, 60, 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
  • 32
    • 84986446950 scopus 로고
    • Microbial transglutaminase and ∈-(γ-glutamyl)lysine crosslink effects on elastic properties of kamaboko gels
    • Seguro, K., Kumazawa, Y., Ohtsuka, T., Toiguchi, S. Motoki, M. (1995). Microbial transglutaminase and ∈-(γ-glutamyl)lysine crosslink effects on elastic properties of kamaboko gels. Journal of Food Science, 60, 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
  • 33
    • 0032429619 scopus 로고    scopus 로고
    • Disulfide bonds influence the heat-induced gel properties of chicken breast muscle myosin
    • Smyth, A.B., Smith, D.M. O'Neill, E. (1998). Disulfide bonds influence the heat-induced gel properties of chicken breast muscle myosin. Journal of Food Science, 63, 584 587.
    • (1998) Journal of Food Science , vol.63 , pp. 584-587
    • Smyth, A.B.1    Smith, D.M.2    O'Neill, E.3
  • 34
    • 0000118723 scopus 로고    scopus 로고
    • Characterization of active components in food-grade proteinase inhibitors for surimi manufacture
    • Weerasinghe, V.C., Morrissey, M.T. An, H. (1996). Characterization of active components in food-grade proteinase inhibitors for surimi manufacture. Journal of Agricultural and Food Chemistry, 44, 2584 2590.
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 2584-2590
    • Weerasinghe, V.C.1    Morrissey, M.T.2    An, H.3
  • 35
    • 0036266368 scopus 로고    scopus 로고
    • Biochemical and conformation changes of actomyosin from Threadfin bream stored in ice
    • Yongsawatdigul, J. Park, J.W. (2002). Biochemical and conformation changes of actomyosin from Threadfin bream stored in ice. Journal of Food Science, 67, 985 990.
    • (2002) Journal of Food Science , vol.67 , pp. 985-990
    • Yongsawatdigul, J.1    Park, J.W.2
  • 36
    • 2442562651 scopus 로고    scopus 로고
    • Inhibition of autolytic activity of lizardfish surimi by proteinase inhibitors
    • Yongsawatdigul, J. Piyadhammaviboon, P. (2004). Inhibition of autolytic activity of lizardfish surimi by proteinase inhibitors. Food Chemistry, 87, 447 455.
    • (2004) Food Chemistry , vol.87 , pp. 447-455
    • Yongsawatdigul, J.1    Piyadhammaviboon, P.2


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