메뉴 건너뛰기




Volumn 14, Issue 2, 2008, Pages 167-177

The effect of washing, microbial transglutaminase, salts and starch addition on the functional properties of sardine (Sardina Pilchardus) kamaboko gels

Author keywords

Differential scanning calorimetry (DSC); Functional properties; Gelation; Kamaboko; MTGase; Sardine surimi

Indexed keywords

ADDITION REACTIONS; COLLOIDS; GELATION; GELS; WASHING;

EID: 45849135260     PISSN: 10820132     EISSN: 15321738     Source Type: Journal    
DOI: 10.1177/1082013208092816     Document Type: Article
Times cited : (12)

References (34)
  • 2
    • 0242490912 scopus 로고    scopus 로고
    • Suwari gel properties as affected by transglutaminase activator and inhibitors
    • Benjakul S., Visessanguan W. and Pecharat S. (2004). Suwari gel properties as affected by transglutaminase activator and inhibitors. Food Chemistry 85: 91-99.
    • (2004) Food Chemistry , vol.85 , pp. 91-99
    • Benjakul, S.1    Visessanguan, W.2    Pecharat, S.3
  • 3
    • 4644370457 scopus 로고    scopus 로고
    • Characteristics and gel properties of muscles from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) caught in Thailand
    • Chaijan M., Benjakul S., Visessanguan W. and Faustman C. (2004). Characteristics and gel properties of muscles from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) caught in Thailand. Food Research International 37: 1021-1030.
    • (2004) Food Research International , vol.37 , pp. 1021-1030
    • Chaijan, M.1    Benjakul, S.2    Visessanguan, W.3    Faustman, C.4
  • 4
    • 0008638344 scopus 로고    scopus 로고
    • Effect of non-muscle protein on the thermogelation of horse mackerel surimi and the resultant cooking tolerance of kamaboko
    • Chen H.H. (2000). Effect of non-muscle protein on the thermogelation of horse mackerel surimi and the resultant cooking tolerance of kamaboko. Fisheries Science 66: 783-788.
    • (2000) Fisheries Science , vol.66 , pp. 783-788
    • Chen, H.H.1
  • 5
    • 0030656353 scopus 로고    scopus 로고
    • Colour and gel-forming properties of horse mackerel (Trachurus japonicus) as related to washing conditions
    • Chen H.H., Chiu E.M. and Huang J.R. (1997). Colour and gel-forming properties of horse mackerel (Trachurus japonicus) as related to washing conditions. Journal of Food Science 62: 985-991.
    • (1997) Journal of Food Science , vol.62 , pp. 985-991
    • Chen, H.H.1    Chiu, E.M.2    Huang, J.R.3
  • 7
    • 33746350356 scopus 로고    scopus 로고
    • Surimi resources
    • Park J.W. (ed.), New York: Taylor and Francis, pp.
    • Guenneugues P. and Morrissey M.T. (2004). Surimi resources. In: Park J. W. (ed.), Surimi and Surimi Seafood. New York: Taylor and Francis, pp. 3-32.
    • (2004) Surimi and Surimi Seafood , pp. 3-32
    • Guenneugues, P.1    Morrissey, M.T.2
  • 8
    • 0012698485 scopus 로고
    • Viscoelastic properties of surimi seafood products
    • Rao M.A. and Steffe J.F. (eds), New York: Elsevier Applied Science, pp.
    • Hamann D.D. (1992). Viscoelastic properties of surimi seafood products. In: Rao M.A. and Steffe J.F. (eds), Viscoelastic Properties of Foods. New York: Elsevier Applied Science, pp. 157-171.
    • (1992) Viscoelastic Properties of Foods , pp. 157-171
    • Hamann, D.D.1
  • 9
    • 0002454157 scopus 로고    scopus 로고
    • Surimi processing from dark muscle fish
    • Park J.W. (ed.), New York: Marcel Dekker Inc, pp.
    • Hultin H.O. and Kelleher S.D. (2000). Surimi processing from dark muscle fish. In: Park J.W. (ed.), Surimi and Surimi Seafood, New York: Marcel Dekker Inc, pp. 59-77.
    • (2000) Surimi and Surimi Seafood , pp. 59-77
    • Hultin, H.O.1    Kelleher, S.D.2
  • 11
    • 84919691716 scopus 로고
    • Temperature and pH affect transglutaminase-catalyzed ''setting'' of crude fish actomyosin
    • Joseph D., Lanier T.C. and Hamann D.D. (1994). Temperature and pH affect transglutaminase-catalyzed ''setting'' of crude fish actomyosin. Journal of Food Science 59: 1018-1023, 1036.
    • (1994) Journal of Food Science , vol.59 , pp. 1018-1023
    • Joseph, D.1    Lanier, T.C.2    Hamann, D.D.3
  • 12
    • 43649103040 scopus 로고    scopus 로고
    • The effect of initial wash at acidic and alkaline pHs on the properties of protein concentrate (kamaboko) products from sardine (Sardina pilchardus) samples
    • Karayannakidis P.D., Zotos A., Petridis D. and Taylor K. D.A. (2007). The effect of initial wash at acidic and alkaline pHs on the properties of protein concentrate (kamaboko) products from sardine (Sardina pilchardus) samples. Journal of Food Engineering 78: 775-783.
    • (2007) Journal of Food Engineering , vol.78 , pp. 775-783
    • Karayannakidis, P.D.1    Zotos, A.2    Petridis, D.3    Taylor, K.4
  • 14
    • 0001522023 scopus 로고
    • Suppression of surimi gel setting by transglutaminase inhibitors
    • Kumazawa Y., Numazawa T., Seguro K. and Motoki M. (1995). Suppression of surimi gel setting by transglutaminase inhibitors. Journal of Food Science 60: 715-717, 726.
    • (1995) Journal of Food Science , vol.60 , pp. 715-717
    • Kumazawa, Y.1    Numazawa, T.2    Seguro, K.3    Motoki, M.4
  • 15
    • 0002836045 scopus 로고
    • Measurement of surimi composition and functional properties
    • Lanier T.C. and Lee C.M. (eds), New York: Marcel Dekker Inc., pp.
    • Lanier T.C. (1992). Measurement of surimi composition and functional properties. In: Lanier T.C. and Lee C. M. (eds), Surimi Technology. New York: Marcel Dekker Inc., pp. 123-163.
    • (1992) Surimi Technology , pp. 123-163
    • Lanier, T.C.1
  • 16
    • 33748339636 scopus 로고    scopus 로고
    • Surimi gelation chemistry
    • Park J.W. (ed.), New York: Taylor and Francis, pp.
    • Lanier T.C., Carvajal P. and Yongsawatdigul J. (2004). Surimi gelation chemistry. In: Park J.W. (ed.), Surimi and Surimi Seafood, New York: Taylor and Francis, pp. 435-489.
    • (2004) Surimi and Surimi Seafood , pp. 435-489
    • Lanier, T.C.1    Carvajal, P.2    Yongsawatdigul, J.3
  • 17
    • 0030803491 scopus 로고    scopus 로고
    • Transglutaminase effects on low temperature gelation of fish protein sols
    • Lee H.G., Lanier T.C., Hamann D.D. and 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
  • 18
    • 0007886372 scopus 로고
    • Applications of differential scanning calorimetry in foods
    • Peleg M. and Bugley E.B. (eds), Westport, Connecticut: AVI Publishing Company Inc, pp.
    • Lund D.B. (1983). Applications of differential scanning calorimetry in foods. In: Peleg M. and Bugley E.B. (eds), Physical Properties of Foods. Westport, Connecticut: AVI Publishing Company Inc, pp. 125-143.
    • (1983) Physical Properties of Foods , pp. 125-143
    • Lund, D.B.1
  • 19
    • 0000823168 scopus 로고    scopus 로고
    • Protein gelation
    • Damodaran S. and Paraf A. (eds), New York: Marcel Dekker Inc, pp.
    • Oakenfull D., Pearce J. and Burley R.W. (1997). Protein gelation. In: Damodaran S. and Paraf A. (eds), Food Proteins and Their Applications. New York: Marcel Dekker Inc, pp. 111-142.
    • (1997) Food Proteins and Their Applications , pp. 111-142
    • Oakenfull, D.1    Pearce, J.2    Burley, R.W.3
  • 20
    • 0034923343 scopus 로고    scopus 로고
    • Effect of alkaline and acidic wash treatments on functional properties and color of Monterey sardine (Sardinops sagax caerulea) minced flesh
    • Pacheco-Aguilar R., Ramez-Surez, JC, Mazorra-Manzano MA (2001). Effect of alkaline and acidic wash treatments on functional properties and color of Monterey sardine (Sardinops sagax caerulea) minced flesh. Journal of Aquatic Food Production and Technology 10: 85-99.
    • (2001) Journal of Aquatic Food Production and Technology , vol.10 , pp. 85-99
    • Pacheco-Aguilar, R.1    Ramez-Surez, J.C.2    Ma, M.3
  • 21
    • 84986465438 scopus 로고
    • Surimi gel colors as affected by moisture content and physical conditions
    • Park J.W. (1995). Surimi gel colors as affected by moisture content and physical conditions. Journal of Food Science 60: 15-18.
    • (1995) Journal of Food Science , vol.60 , pp. 15-18
    • Park, J.W.1
  • 22
    • 33947601680 scopus 로고    scopus 로고
    • Ingredient technology for surimi and surimi seafood
    • Park J.W. (ed.), New York: Taylor and Francis, pp.
    • Park J.W. (2004). Ingredient technology for surimi and surimi seafood. In: Park J.W. (ed.), Surimi and Surimi Seafood. New York: Taylor and Francis, pp. 649-707.
    • (2004) Surimi and Surimi Seafood , pp. 649-707
    • Park, J.W.1
  • 23
    • 33748762209 scopus 로고    scopus 로고
    • Comparison of Atlantic menhaden gels from surimi processed by acid or alkaline solubilization
    • Perez-Mateos M. and Lanier T.C. (2007). Comparison of Atlantic menhaden gels from surimi processed by acid or alkaline solubilization. Food Chemistry 101: 1223-1229.
    • (2007) Food Chemistry , vol.101 , pp. 1223-1229
    • Perez-Mateos, M.1    Lanier, T.C.2
  • 24
    • 0342656216 scopus 로고    scopus 로고
    • Surimi gels from striped mullet (Mugil cephalus) employing microbial transglutaminase
    • Ramrez J.A., Rodrguez-Sosa R., Morales O.G. and Vazquez M. (2000). Surimi gels from striped mullet (Mugil cephalus) employing microbial transglutaminase. Food Chemistry 70: 443-449.
    • (2000) Food Chemistry , vol.70 , pp. 443-449
    • Ramrez, J.A.1    Rodrguez-Sosa, R.2    Morales, O.G.3    Vazquez, M.4
  • 25
    • 0000208426 scopus 로고
    • Surimi production from fatty and darked-fleshed fish species
    • Lanier T.C. and Lee C.M. (eds), New York: Marcel Dekker Inc, pp.
    • Shimizu Y., Haruhiko T. and Lanier T.C. (1992). Surimi production from fatty and darked-fleshed fish species. In: Lanier T.C. and Lee C. M. (eds), Surimi Technology. New York: Marcel Dekker Inc, pp. 181-207.
    • (1992) Surimi Technology , pp. 181-207
    • Shimizu, Y.1    Haruhiko, T.2    Lanier, T.C.3
  • 26
    • 0346575766 scopus 로고
    • Surimi processing from fatty fish
    • Shahidi F. and Botta J.R. (eds), London: Blackie & Academic Professional, pp.
    • Spencer K.E. and Tung M.A. (1994). Surimi processing from fatty fish. In: Shahidi F. and Botta J.R. (eds), Seafoods: Chemistry, Processing Technology and Quality. London: Blackie & Academic Professional, pp. 288-319.
    • (1994) Seafoods: Chemistry, Processing Technology and Quality , pp. 288-319
    • Spencer, K.E.1    Tung, M.A.2
  • 27
    • 0034123017 scopus 로고    scopus 로고
    • Microbiological and color quality changes of channel catfish frame mince during chilled and frozen storage
    • Suvanich V., Marshall D.L. and Jahncke M.L. (2000). Microbiological and color quality changes of channel catfish frame mince during chilled and frozen storage. Journal of Food Science 65: 151-154.
    • (2000) Journal of Food Science , vol.65 , pp. 151-154
    • Suvanich, V.1    Marshall, D.L.2    Jahncke, M.L.3
  • 28
    • 84985200374 scopus 로고
    • Thermal transitions of actomyosin and surimi prepared from Atlantic croaker as studied by differential scanning calorimetry
    • Wu M.C., Akahane T., Lanier T.C. and Hamann D.D. (1985 b). Thermal transitions of actomyosin and surimi prepared from Atlantic croaker as studied by differential scanning calorimetry. Journal of Food Science 50: 10-13.
    • (1985) Journal of Food Science , vol.50 , pp. 10-13
    • Wu, M.C.1    Akahane, T.2    Lanier, T.C.3    Hamann, D.D.4
  • 29
    • 84981407132 scopus 로고
    • Rheological and calorimetric investigations of starch-fish protein systems during thermal processing
    • Wu M.C., Hamann D.D. and Lanier T.C. (1985 d). Rheological and calorimetric investigations of starch-fish protein systems during thermal processing. Journal of Texture Studies 16: 53-74.
    • (1985) Journal of Texture Studies , vol.16 , pp. 53-74
    • Wu, M.C.1    Hamann, D.D.2    Lanier, T.C.3
  • 30
    • 84985280176 scopus 로고
    • Thermal transitions of admixed starch/fish protein systems during heating
    • Wu M.C., Lanier T.C. and Hamann D.D. (1985 a). 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
  • 31
    • 0009837636 scopus 로고
    • Rigidity and viscosity changes of croaker actomyosin during thermal gelation
    • Wu M.C., Lanier T.C. and Hamann D.D. (1985 c) Rigidity and viscosity changes of croaker actomyosin during thermal gelation. Journal of Food Science 50: 14-19, 25.
    • (1985) Journal of Food Science , vol.50 , pp. 14-19
    • Wu, M.C.1    Lanier, T.C.2    Hamann, D.D.3
  • 32
    • 0012476349 scopus 로고    scopus 로고
    • Effects of starch properties and thermal-processing conditions on surimi-starch gels
    • Yang H. and Park J.W. (1998). Effects of starch properties and thermal-processing conditions on surimi-starch gels. Lebensmittel -Wissenschaft und Technologie 31: 344-353.
    • (1998) Lebensmittel -Wissenschaft und Technologie , vol.31 , pp. 344-353
    • Yang, H.1    Park, J.W.2
  • 33
    • 4744341461 scopus 로고    scopus 로고
    • Effects of alkali and acid solubilization on gelation characteristics of rockfish muscle proteins
    • Yongsawatdigul J. and Park J.W. (2004). Effects of alkali and acid solubilization on gelation characteristics of rockfish muscle proteins. Journal of Food Science 69: 495-505.
    • (2004) Journal of Food Science , vol.69 , pp. 495-505
    • Yongsawatdigul, J.1    Park, J.W.2
  • 34
    • 0004252445 scopus 로고
    • 2nd edn, New Jersey: Prentice Hall Inc.
    • Zar J.H. (1984). Biostatistical analysis. 2 nd edn, New Jersey: Prentice Hall Inc.
    • (1984) Biostatistical Analysis
    • Zar, J.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.