메뉴 건너뛰기




Volumn 41, Issue 2, 2010, Pages 153-170

A comparative study on physical properties and chemical interactions of gels from tilapia meat pastes induced by heat and pressure

Author keywords

Chemical interaction; Gel forming ability; Heat; Hydrostatic pressure; Rheological property

Indexed keywords

TILAPIA;

EID: 77954473729     PISSN: 00224901     EISSN: 17454603     Source Type: Journal    
DOI: 10.1111/j.1745-4603.2010.00219.x     Document Type: Article
Times cited : (61)

References (30)
  • 1
    • 0000873463 scopus 로고
    • Heat-induced gelation of minced rainbow trout (Salmo gairdneri): Effect of pH, sodium chloride and setting
    • AUTIO K, KIESVAARA M, POLVINEN K. Heat-induced gelation of minced rainbow trout (Salmo gairdneri): Effect of pH, sodium chloride and setting. J. Food Sci. 1989, 54:805-823.
    • (1989) J. Food Sci. , vol.54 , pp. 805-823
    • Autio, K.1    Kiesvaara, M.2    Polvinen, K.3
  • 2
    • 21344491096 scopus 로고
    • Effects of high pressure on proteins.
    • BALNY C, MASSON P. Effects of high pressure on proteins. Food Rev. Int. 1993, 9:611-628.
    • (1993) Food Rev. Int. , vol.9 , pp. 611-628
    • Balny, C.1    Masson, P.2
  • 3
    • 84985294638 scopus 로고
    • Effects of heat-stable alkaline protease activity of Atlantic menhaden (Brevoorti tyrannus) on surimi gels
    • BOYE SW, LANIER TC. Effects of heat-stable alkaline protease activity of Atlantic menhaden (Brevoorti tyrannus) on surimi gels. J. Food Sci. 1988, 53:1340-1398.
    • (1988) J. Food Sci. , vol.53 , pp. 1340-1398
    • Boye, S.W.1    Lanier, T.C.2
  • 4
    • 0010036861 scopus 로고
    • High pressure gelation of fish myofibrillar proteins
    • Dickinson E, Lorient D. In, eds., Royal Society of Chemistry, London, U.K
    • CARLEZ A, BORDERIAS AJ, DUMAY E, CHEFTEL JC. High pressure gelation of fish myofibrillar proteins. Food Macromolecules and Colloids 1995, Dickinson E, Lorient D, In, eds., Royal Society of Chemistry, London, U.K
    • (1995) Food Macromolecules and Colloids
    • Carlez, A.1    Borderias, A.J.2    Dumay, E.3    Cheftel, J.C.4
  • 5
    • 84986505834 scopus 로고
    • Herring surimi during low temperature setting, physicochemical and textural properties
    • CHAN JK, GILL TA, THOMPSON JW, SINGER DS. Herring surimi during low temperature setting, physicochemical and textural properties. J. Food Sci. 1995, 60:1248-1253.
    • (1995) J. Food Sci. , vol.60 , pp. 1248-1253
    • Chan, J.K.1    Gill, T.A.2    Thompson, J.W.3    Singer, D.S.4
  • 6
    • 84987313521 scopus 로고
    • Proteolytic activity of surimi from Pacific whiting (Merluccius productus) and heat-set gel texture
    • CHANG-LEE MV, PACHECO-AGUILAR R, CRAWFORD DL, LAMPILA LE. Proteolytic activity of surimi from Pacific whiting (Merluccius productus) and heat-set gel texture. J. Food Sci. 1989, 54:1116-1119.
    • (1989) J. Food Sci. , vol.54 , pp. 1116-1119
    • Chang-Lee, M.V.1    Pacheco-Aguilar, R.2    Crawford, D.L.3    Lampila, L.E.4
  • 7
    • 0000872633 scopus 로고
    • Effects of high hydrostatic pressure on food constituents: An overview
    • Balny C. In, ed., John Libbey Eurotext Ltd., London, England
    • CHEFTEL JC. Effects of high hydrostatic pressure on food constituents: An overview. High Pressure and Biotechnology 1992, Balny C. In, ed., John Libbey Eurotext Ltd., London, England
    • (1992) High Pressure and Biotechnology
    • Cheftel, J.C.1    et al2
  • 8
    • 0031190812 scopus 로고    scopus 로고
    • Effects of high pressure on meat: A review.
    • CHEFTEL JC, CULIOLI J. Effects of high pressure on meat: A review. Meat Sci. 1997, 46:211-236.
    • (1997) Meat Sci. , vol.46 , pp. 211-236
    • Cheftel, J.C.1    Culioli, J.2
  • 10
    • 0024786754 scopus 로고
    • Thermal aggregation of cod (Gadus morhua) muscle proteins using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a zero length cross-linker
    • GILL TA, CONWAY JT. Thermal aggregation of cod (Gadus morhua) muscle proteins using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a zero length cross-linker. Agric. Biol. Chem. 1989, 53:2553-2562.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 2553-2562
    • Gill, T.A.1    Conway, J.T.2
  • 11
    • 14444282417 scopus 로고    scopus 로고
    • Covalent bonding in pressure-induced fish protein gels
    • GILLELAND GM, LANIER TC, HAMANN DD. Covalent bonding in pressure-induced fish protein gels. J. Food Sci. 1997, 62(4):733-716.
    • (1997) J. Food Sci. , vol.62 , Issue.4 , pp. 733-1716
    • Gilleland, G.M.1    Lanier, T.C.2    Hamann, D.D.3
  • 13
    • 33847786505 scopus 로고    scopus 로고
    • Effect of pretreatment of hydrostatic pressure on physicochemical properties of tilapia muscle protein gels induced by setting
    • HSU KC, JAO CL. Effect of pretreatment of hydrostatic pressure on physicochemical properties of tilapia muscle protein gels induced by setting. J. Food Sci. 2007, 72:E73-E78.
    • (2007) J. Food Sci. , vol.72
    • Hsu, K.C.1    Jao, C.L.2
  • 14
    • 0035661783 scopus 로고    scopus 로고
    • Effect of hydrostatic pressure on aggregation and viscoelastic properties of tilapia (Orechromis niloticus) myosin
    • HSU KC, KO WC. Effect of hydrostatic pressure on aggregation and viscoelastic properties of tilapia (Orechromis niloticus) myosin. J. Food Sci. 2001, 66:1158-1162.
    • (2001) J. Food Sci. , vol.66 , pp. 1158-1162
    • Hsu, K.C.1    Ko, W.C.2
  • 15
    • 34247501186 scopus 로고    scopus 로고
    • Changes in textural and rheological properties of gels from tilapia muscle proteins induced by high pressure and setting
    • HWANG JS, LAI KM, HSU KC. Changes in textural and rheological properties of gels from tilapia muscle proteins induced by high pressure and setting. Food Chem. 2007, 104:746-753.
    • (2007) Food Chem. , vol.104 , pp. 746-753
    • Hwang, J.S.1    Lai, K.M.2    Hsu, K.C.3
  • 16
    • 0001011970 scopus 로고
    • Dynamic rheological measurements on heat-induced pressurized actomyosin gels
    • IKEUCHI Y, TANJI H, KIM K, SUZUKI A. Dynamic rheological measurements on heat-induced pressurized actomyosin gels. J. Agric. Food Chem. 1992, 40:1751-1755.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 1751-1755
    • Ikeuchi, Y.1    Tanji, H.2    Kim, K.3    Suzuki, A.4
  • 17
    • 0038528591 scopus 로고    scopus 로고
    • Effect of hydrostatic pressure on the molecular conformation of tilapia (Orechromis niloticus) myosin
    • KO WC, JAO CL, HSU KC. Effect of hydrostatic pressure on the molecular conformation of tilapia (Orechromis niloticus) myosin. J. Food Sci. 2003, 68:1192-1195.
    • (2003) J. Food Sci. , vol.68 , pp. 1192-1195
    • Ko, W.C.1    Jao, C.L.2    Hsu, K.C.3
  • 18
    • 85014938976 scopus 로고
    • The role of covalent crosslinking in the texturizing of muscle protein sols
    • LEE H, LANIER TC. The role of covalent crosslinking in the texturizing of muscle protein sols. J. Muscle Foods 1995, 6:125-138.
    • (1995) J. Muscle Foods , vol.6 , pp. 125-138
    • Lee, H.1    Lanier, T.C.2
  • 20
    • 0000046977 scopus 로고    scopus 로고
    • Comparison of different gelation methods using washed sardine (Sardina pilchardus) mince: Effects of temperature and pressure
    • MONTERO P, PÉREZ-MATEOS M, SOLAS T. Comparison of different gelation methods using washed sardine (Sardina pilchardus) mince: Effects of temperature and pressure. J. Agric. Food Chem. 1997, 45:4612-4618.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 4612-4618
    • Montero, P.1    Pérez-Mateos, M.2    Solas, T.3
  • 21
    • 0000076551 scopus 로고
    • Setting of mixed salted meat paste of two fish species in relation to cross-linking reaction of myosin heavy chain
    • NISHIMOTO SI, HASHIMOTO A, SEKI N, ARAI KI. Setting of mixed salted meat paste of two fish species in relation to cross-linking reaction of myosin heavy chain. Nippon Suisan Gakkaishi 1988, 54:1227-1235.
    • (1988) Nippon Suisan Gakkaishi , vol.54 , pp. 1227-1235
    • Nishimoto, S.I.1    Hashimoto, A.2    Seki, N.3    Arai, K.I.4
  • 22
    • 0001488282 scopus 로고
    • Participation of S-S bonding in the appearance of setting
    • NIWA E, MATUSBARA Y, HAMADA Y. Participation of S-S bonding in the appearance of setting. Nippon Suisan Gakkaishi 1982, 49:727.
    • (1982) Nippon Suisan Gakkaishi , vol.49 , pp. 727
    • Niwa, E.1    Matusbara, Y.2    Hamada, Y.3
  • 23
    • 84872885475 scopus 로고
    • Application of high pressure to food processing: Textural comparison of pressure- and heat-induced gels of food proteins
    • OKAMOTO M, KAWAMURA Y, HAYASHI R. Application of high pressure to food processing: Textural comparison of pressure- and heat-induced gels of food proteins. Agric. Biol. Chem. 1990, 54:183-189.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 183-189
    • Okamoto, M.1    Kawamura, Y.2    Hayashi, R.3
  • 24
    • 0002083553 scopus 로고    scopus 로고
    • Rheological and biochemical characteristic of high pressure and heat-induced gels from blue whiting (Micromesistius poutassou) muscle protein
    • PÉREZ-MATEOS M, LOURENÇO H, MONTERO P, BORDERIAS J. Rheological and biochemical characteristic of high pressure and heat-induced gels from blue whiting (Micromesistius poutassou) muscle protein. J. Agric. Food Chem. 1997, 45:44-49.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 44-49
    • Pérez-Mateos, M.1    Lourenço, H.2    Montero, P.3    Borderias, J.4
  • 25
    • 85005716785 scopus 로고
    • Mechanisms of gelation of sardine proteins: Influence of thermal processing and of various additives on the texture and protein solubility of kamaboko gels
    • ROUSSEL H, CHEFTEL JC. Mechanisms of gelation of sardine proteins: Influence of thermal processing and of various additives on the texture and protein solubility of kamaboko gels. Int. J. Food Sci. Tech. 1990, 25:260-280.
    • (1990) Int. J. Food Sci. Tech. , vol.25 , pp. 260-280
    • Roussel, H.1    Cheftel, J.C.2
  • 26
    • 0000845463 scopus 로고
    • Gel forming characteristics of frozen surimi from chum salmon in the presence of protease inhibitors
    • SAEKI H, ISEYA Z, SUGIURA S, SEKI N. Gel forming characteristics of frozen surimi from chum salmon in the presence of protease inhibitors. J. Food Sci. 1995, 60:917-921.
    • (1995) J. Food Sci. , vol.60 , pp. 917-921
    • Saeki, H.1    Iseya, Z.2    Sugiura, S.3    Seki, N.4
  • 28
    • 0040802102 scopus 로고    scopus 로고
    • Comparative properties of bluefish (Pomatomus saltatrix) gels formulated by high hydrostatic pressure and heat
    • SAREEVORAVITKUL R, SIMPSON BK, RAMASWAMY HS. Comparative properties of bluefish (Pomatomus saltatrix) gels formulated by high hydrostatic pressure and heat. J. Aquat. Food Prod. Tech. 1996, 5:65-79.
    • (1996) J. Aquat. Food Prod. Tech. , vol.5 , pp. 65-79
    • Sareevoravitkul, R.1    Simpson, B.K.2    Ramaswamy, H.S.3
  • 29
    • 0032926829 scopus 로고    scopus 로고
    • Physical characteristics of surimi seafood as affected by thermal processing conditions
    • SHIE JS, PARK JW. Physical characteristics of surimi seafood as affected by thermal processing conditions. J. Food Sci. 1999, 64:287-290.
    • (1999) J. Food Sci. , vol.64 , pp. 287-290
    • Shie, J.S.1    Park, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.