메뉴 건너뛰기




Volumn 69, Issue 1, 2004, Pages

Physicochemical Changes in Alaska Pollock Surimi and Surimi Gel as Affected by Electron Beam

Author keywords

E beam; Protein gelation; SDS PAGE; Shear stress; Surimi

Indexed keywords

POLLACHIUS VIRENS; THERAGRA CHALCOGRAMMA;

EID: 1242344869     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2004.tb17855.x     Document Type: Article
Times cited : (65)

References (35)
  • 1
    • 0034001548 scopus 로고    scopus 로고
    • Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes
    • Alizadeh-Pasdar N, Li-Chan ECY. 2000. Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes. J Agric Food Chem 48:328-34.
    • (2000) J Agric Food Chem , vol.48 , pp. 328-334
    • Alizadeh-Pasdar, N.1    Li-Chan, E.C.Y.2
  • 2
    • 84986437097 scopus 로고
    • Surimi-based imitation crab characteristics affected by heating method and end point temperature
    • Bertak JA, Karahadian C. 1995. Surimi-based imitation crab characteristics affected by heating method and end point temperature. J Food Sci 60(2):292-6.
    • (1995) J Food Sci , vol.60 , Issue.2 , pp. 292-296
    • Bertak, J.A.1    Karahadian, C.2
  • 4
    • 0031433220 scopus 로고    scopus 로고
    • Structural changes in cod myosin after modification with formaldehyde or frozen storage
    • Careche M, Li-Chan ECY. 1997. Structural changes in cod myosin after modification with formaldehyde or frozen storage. J Food Sci 62(4):717-22.
    • (1997) J Food Sci , vol.62 , Issue.4 , pp. 717-722
    • Careche, M.1    Li-Chan, E.C.Y.2
  • 5
    • 84987300695 scopus 로고
    • Textural changes in precooked lobster (Homarus americanus) meat resulting from radurization followed by refrigerated storage
    • Dagbjartsson B, Solberg M. 1973. Textural changes in precooked lobster (Homarus americanus) meat resulting from radurization followed by refrigerated storage. J Food Sci 28:165-7.
    • (1973) J Food Sci , vol.28 , pp. 165-167
    • Dagbjartsson, B.1    Solberg, M.2
  • 7
    • 0000734038 scopus 로고
    • Gamma radiation effects on shelf life and gel forming properties of washed Red Hake (Urophycis chuss) fish mince
    • Dymsza HA, Lee CM, Saibu LO, Haun J, Silverman GJ, Josephson ES. 1990. Gamma radiation effects on shelf life and gel forming properties of washed Red Hake (Urophycis chuss) fish mince. J Food Sci 55(6):1745-8.
    • (1990) J Food Sci , vol.55 , Issue.6 , pp. 1745-1748
    • Dymsza, H.A.1    Lee, C.M.2    Saibu, L.O.3    Haun, J.4    Silverman, G.J.5    Josephson, E.S.6
  • 8
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman GL. 1959. Tissue sulfhydryl groups. Arch Biochem Biophys 82:70-7.
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 10
    • 0002482686 scopus 로고
    • Structural failure in solid foods
    • Bagley EB. Peleg M. editors. Westport, Conn.: AVI Publishing Co.
    • Hamann DD. 1983. Structural failure in solid foods. In: Bagley EB. Peleg M. editors. Physical properties of foods. Westport, Conn.: AVI Publishing Co. p 351-83.
    • (1983) Physical Properties of Foods , pp. 351-383
    • Hamann, D.D.1
  • 11
    • 85008112707 scopus 로고
    • Effect of ultraviolet radiation on rheological properties of thermal gels from sardine and pork meat pastes
    • Ishizaki S, Hamada M, Iso N, Taguchi T. 1993. Effect of ultraviolet radiation on rheological properties of thermal gels from sardine and pork meat pastes. Nipp Suis Gakkai 59(7):1219-24.
    • (1993) Nipp Suis Gakkai , vol.59 , Issue.7 , pp. 1219-1224
    • Ishizaki, S.1    Hamada, M.2    Iso, N.3    Taguchi, T.4
  • 12
    • 85032070646 scopus 로고
    • Ultraviolet denaturation of flying fish myosin and its fragments
    • Ishizaki S, Ogasawara M, Tanaka M, Taguchi T. 1994. Ultraviolet denaturation of flying fish myosin and its fragments. Fisheries Science 60(5):603-6.
    • (1994) Fisheries Science , vol.60 , Issue.5 , pp. 603-606
    • Ishizaki, S.1    Ogasawara, M.2    Tanaka, M.3    Taguchi, T.4
  • 13
    • 85008054299 scopus 로고
    • Behavior of the sulfhydryl groups of carp actomyosin by heating
    • Itoh Y, Yoshinaka R, Ikeda S. 1979. Behavior of the sulfhydryl groups of carp actomyosin by heating. Nipp Suis Gakkai 45:1019-22.
    • (1979) Nipp Suis Gakkai , vol.45 , pp. 1019-1022
    • Itoh, Y.1    Yoshinaka, R.2    Ikeda, S.3
  • 14
    • 85004503526 scopus 로고
    • Formation of polymeric molecules of protein resulting from intermolecular SS bonds formed during the gel formation of carp actomyosin by heting
    • Itoh Y, Yoshinaka R, Ikeda S. 1980. Formation of polymeric molecules of protein resulting from intermolecular SS bonds formed during the gel formation of carp actomyosin by heting. Nipp Suis Gakkai 46:621-4.
    • (1980) Nipp Suis Gakkai , vol.46 , pp. 621-624
    • Itoh, Y.1    Yoshinaka, R.2    Ikeda, S.3
  • 15
    • 0038234765 scopus 로고    scopus 로고
    • Microbial inactivation and electron penetration in surimi seafood during electron beam processing
    • Jaczynski J, Park JW. 2003a. Microbial inactivation and electron penetration in surimi seafood during electron beam processing. J Food Sci 68(5):1788-92.
    • (2003) J Food Sci , vol.68 , Issue.5 , pp. 1788-1792
    • Jaczynski, J.1    Park, J.W.2
  • 16
    • 0038300742 scopus 로고    scopus 로고
    • Physicochemical properties of surimi seafood as affected by electron beam and heat
    • Jaczynski J, Park JW. 2003b. Physicochemical properties of surimi seafood as affected by electron beam and heat. J Food Sci 68(5):1626-30.
    • (2003) J Food Sci , vol.68 , Issue.5 , pp. 1626-1630
    • Jaczynski, J.1    Park, J.W.2
  • 17
    • 0000730592 scopus 로고    scopus 로고
    • Cross-linking of mackerel surimi actomyosin by microbial transglutamizase and ultraviolet radiation
    • Jiang ST, Leu SZ, Tsai GJ. 1998. Cross-linking of mackerel surimi actomyosin by microbial transglutamizase and ultraviolet radiation. J Agric Food Chem 46:5278-82.
    • (1998) J Agric Food Chem , vol.46 , pp. 5278-5282
    • Jiang, S.T.1    Leu, S.Z.2    Tsai, G.J.3
  • 18
    • 84986449596 scopus 로고
    • Chemical and physical changes in irradiated and frozen bombay duck
    • Kumta US, Gore MS. 1970. Chemical and physical changes in irradiated and frozen bombay duck. J Food Sci 35:456-60.
    • (1970) J Food Sci , vol.35 , pp. 456-460
    • Kumta, U.S.1    Gore, M.S.2
  • 19
    • 0001554239 scopus 로고    scopus 로고
    • Surimi gelation chemistry
    • Park JW, editor. New York: Marcel Dekker
    • Lanier TC. 2000. Surimi gelation chemistry. In: Park JW, editor. Surimi and surimi seafood. New York: Marcel Dekker. p 237-67.
    • (2000) Surimi and Surimi Seafood , pp. 237-267
    • Lanier, T.C.1
  • 20
    • 85014938976 scopus 로고
    • The role of covalent crosslinking in the texturizing of the muscle proteins sols
    • Lee H, Lanier TC. 1995. The role of covalent crosslinking in the texturizing of the muscle proteins sols. J Muscle Foods 6:125-38.
    • (1995) J Muscle Foods , vol.6 , pp. 125-138
    • Lee, H.1    Lanier, T.C.2
  • 22
    • 0002915720 scopus 로고
    • Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins
    • Monahan FJ, German JB, Kinsella JE. 1995. Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins. J Agric Food Chem 43:46-52.
    • (1995) J Agric Food Chem , vol.43 , pp. 46-52
    • Monahan, F.J.1    German, J.B.2    Kinsella, J.E.3
  • 23
    • 84893743812 scopus 로고
    • Protease inhibitor effect on torsion measurements and autolysis of Pacific whiting surimi
    • Morrissey MT, Wu JW, Lin D, An H. 1993. Protease inhibitor effect on torsion measurements and autolysis of Pacific whiting surimi. J Food Sci 58:1050-4.
    • (1993) J Food Sci , vol.58 , pp. 1050-1054
    • Morrissey, M.T.1    Wu, J.W.2    Lin, D.3    An, H.4
  • 25
    • 0000791007 scopus 로고    scopus 로고
    • Surimi seafood: Products, market, and manufacturing
    • Park JW, editor. New York: Marcel Dekker
    • Park JW. 2000. Surimi seafood: products, market, and manufacturing. In: Park JW, editor. Surimi and surimi seafood. New York: Marcel Dekker. p 213-5.
    • (2000) Surimi and Surimi Seafood , pp. 213-215
    • Park, J.W.1
  • 26
    • 84985261721 scopus 로고
    • Rheological behavior and potential cross-linking of Pacific whiting (Merluccius productus) surimi gel
    • Park JW, Yongsawatdigul J, Lin TM. 1994. Rheological behavior and potential cross-linking of Pacific whiting (Merluccius productus) surimi gel. J Food Sci 59(4):773-6.
    • (1994) J Food Sci , vol.59 , Issue.4 , pp. 773-776
    • Park, J.W.1    Yongsawatdigul, J.2    Lin, T.M.3
  • 27
    • 0032926829 scopus 로고    scopus 로고
    • Physical characteristics of surimi seafood as affected by thermal processing conditions
    • Shie JS, Park JW. 1999. Physical characteristics of surimi seafood as affected by thermal processing conditions. J Food Sci 64(2):287-90.
    • (1999) J Food Sci , vol.64 , Issue.2 , pp. 287-290
    • Shie, J.S.1    Park, J.W.2
  • 28
    • 0001048082 scopus 로고    scopus 로고
    • Role of SH in polymerization of myosin heavy chain during ice storage of carp actomyosin
    • Sompongse W, Itoh Y, Obatake A. 1996. Role of SH in polymerization of myosin heavy chain during ice storage of carp actomyosin. Fisheries Sci 62:110-3.
    • (1996) Fisheries Sci , vol.62 , pp. 110-113
    • Sompongse, W.1    Itoh, Y.2    Obatake, A.3
  • 29
    • 84987288531 scopus 로고
    • Effect of ultraviolet radiation on thermal gelation of muscle pastes
    • Taguchi T, Ishizaki S, Tanaka M, Nagashima Y, Amano K. 1989. Effect of ultraviolet radiation on thermal gelation of muscle pastes. J Food Sci 54(6):1438-40.
    • (1989) J Food Sci , vol.54 , Issue.6 , pp. 1438-1440
    • Taguchi, T.1    Ishizaki, S.2    Tanaka, M.3    Nagashima, Y.4    Amano, K.5
  • 32
    • 0033194974 scopus 로고    scopus 로고
    • Radiation processing to improve the quality of fishery products
    • Venugopal V, Doke SN, Thomas P. 1999. Radiation processing to improve the quality of fishery products. Crit Rev Food Sci Nutr 39(5):391-440.
    • (1999) Crit Rev Food Sci Nutr , vol.39 , Issue.5 , pp. 391-440
    • Venugopal, V.1    Doke, S.N.2    Thomas, P.3
  • 33
    • 84987359716 scopus 로고
    • Effect of radurization on shear resistance and fragmentation of chicken muscle
    • Whiting RC, Richards JF. 1971. Effect of radurization on shear resistance and fragmentation of chicken muscle. J Food Sci 36:752-5.
    • (1971) J Food Sci , vol.36 , pp. 752-755
    • Whiting, R.C.1    Richards, J.F.2
  • 35
    • 0002567238 scopus 로고
    • Mechanism of gel formation by proteins of muscle tissue
    • Ziegler GR, Acton JC. 1984. Mechanism of gel formation by proteins of muscle tissue. Food Technol 38:77-82.
    • (1984) Food Technol , vol.38 , pp. 77-82
    • Ziegler, G.R.1    Acton, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.