메뉴 건너뛰기




Volumn 291, Issue 3-4, 2009, Pages 210-216

Post mortem changes produced in the muscle of sea bream (Sparus aurata) during ice storage

Author keywords

Calpains; Cytoskeletal proteins; Immunohistochemistry; Muscle; Sea bream; Texture

Indexed keywords

FOOD STORAGE; MUSCLE; TEXTURE;

EID: 67349215110     PISSN: 00448486     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.aquaculture.2009.03.032     Document Type: Article
Times cited : (64)

References (31)
  • 1
    • 85008072402 scopus 로고
    • Post-mortem change of three-dimensional structure of collagen fibrillar network in fish muscle pericellular connective tissues corresponding to post-mortem tenderization
    • Ando M., Yoshimoto Y., Inabu K., Nakagawa T., and Makinodan Y. Post-mortem change of three-dimensional structure of collagen fibrillar network in fish muscle pericellular connective tissues corresponding to post-mortem tenderization. Fish. Sci. 61 (1995) 327-330
    • (1995) Fish. Sci. , vol.61 , pp. 327-330
    • Ando, M.1    Yoshimoto, Y.2    Inabu, K.3    Nakagawa, T.4    Makinodan, Y.5
  • 4
    • 0002133615 scopus 로고
    • Fish flesh structure and the role of collagen-its post-mortem aspects and implications for fish processing
    • Huss H.H., et al. (Ed), Elsevier Science, Amsterdam
    • Bremmer H.A. Fish flesh structure and the role of collagen-its post-mortem aspects and implications for fish processing. In: Huss H.H., et al. (Ed). Quality Assurance in the Fish Industry (1992), Elsevier Science, Amsterdam 39-62
    • (1992) Quality Assurance in the Fish Industry , pp. 39-62
    • Bremmer, H.A.1
  • 5
    • 33748519563 scopus 로고    scopus 로고
    • Effects of gutting and ungutting on microbiological, chemical, and sensory properties of aquacultured seabream (Sparus aurata) and sea bass (Dicentrarchus labrax) stored in ice
    • Cakli S., Kilinc B., Cadun A., Dincer T., and Tolasa S. Effects of gutting and ungutting on microbiological, chemical, and sensory properties of aquacultured seabream (Sparus aurata) and sea bass (Dicentrarchus labrax) stored in ice. Crit. Rev. Food Sci. Nutr. 46 (2006) 519-527
    • (2006) Crit. Rev. Food Sci. Nutr. , vol.46 , pp. 519-527
    • Cakli, S.1    Kilinc, B.2    Cadun, A.3    Dincer, T.4    Tolasa, S.5
  • 6
    • 0030966537 scopus 로고    scopus 로고
    • Desmin in muscle formation and maintenance: knockouts and consequences
    • Capetanaki Y., Milner D.J., and Weitzer G. Desmin in muscle formation and maintenance: knockouts and consequences. Cell Struct. Funct. 22 (1997) 103-116
    • (1997) Cell Struct. Funct. , vol.22 , pp. 103-116
    • Capetanaki, Y.1    Milner, D.J.2    Weitzer, G.3
  • 8
    • 0242405610 scopus 로고    scopus 로고
    • Proteolytic potential in white muscle of sea bass (Dicentrarchus labrax L.) during post mortem storage on ice: time-dependent changes in the activity of the components of the calpain system
    • Delbarre-Ladrat C., Verrez-Bagnis V., Noël J., and Fleurence J. Proteolytic potential in white muscle of sea bass (Dicentrarchus labrax L.) during post mortem storage on ice: time-dependent changes in the activity of the components of the calpain system. Food Chem. 84 (2004) 441-446
    • (2004) Food Chem. , vol.84 , pp. 441-446
    • Delbarre-Ladrat, C.1    Verrez-Bagnis, V.2    Noël, J.3    Fleurence, J.4
  • 9
    • 3242791662 scopus 로고    scopus 로고
    • Relative contribution of calpain and cathepsins to protein degradation in muscle of sea bass (Dicentrarchus labrax L.)
    • Delbarre-Ladrat C., Verrez-Bagnis V., Noël J., and Fleurence J. Relative contribution of calpain and cathepsins to protein degradation in muscle of sea bass (Dicentrarchus labrax L.). Food Chem. 88 (2004) 389-395
    • (2004) Food Chem. , vol.88 , pp. 389-395
    • Delbarre-Ladrat, C.1    Verrez-Bagnis, V.2    Noël, J.3    Fleurence, J.4
  • 10
    • 33747131174 scopus 로고    scopus 로고
    • Trends in postmortem aging in fish: understanding of proteolysis and disorganization of the myofibrillar structure
    • Delbarre-Ladrat C., Chéret R., Taylor R., and Verrez-Bagnis V. Trends in postmortem aging in fish: understanding of proteolysis and disorganization of the myofibrillar structure. Crit. Rev. Food Sci. Nutr. 46 (2006) 409-421
    • (2006) Crit. Rev. Food Sci. Nutr. , vol.46 , pp. 409-421
    • Delbarre-Ladrat, C.1    Chéret, R.2    Taylor, R.3    Verrez-Bagnis, V.4
  • 11
    • 0141920735 scopus 로고    scopus 로고
    • Effects of rearing temperature and strain on sensory characteristics, texture, colour and fat of Artic charr (Salvelinus alpinus)
    • Ginés R., Valdimarsdottir T., Sveinsdottir K., and Thorarensen H. Effects of rearing temperature and strain on sensory characteristics, texture, colour and fat of Artic charr (Salvelinus alpinus). Food Qual. Prefer. 15 (2004) 177-185
    • (2004) Food Qual. Prefer. , vol.15 , pp. 177-185
    • Ginés, R.1    Valdimarsdottir, T.2    Sveinsdottir, K.3    Thorarensen, H.4
  • 12
    • 0025868336 scopus 로고
    • Studies on alpha-actinin/actin interaction in the Z-disk by using calpain
    • Goll D., Dayton W., Singh I., and Robson R. Studies on alpha-actinin/actin interaction in the Z-disk by using calpain. J. Biol. Chem. 266 (1991) 8501-8510
    • (1991) J. Biol. Chem. , vol.266 , pp. 8501-8510
    • Goll, D.1    Dayton, W.2    Singh, I.3    Robson, R.4
  • 14
    • 0001698930 scopus 로고
    • Degradation of proteoglycans in the skeletal muscle of Pacific rockfish (Sebastes sp.) during ice storage
    • Kim K., and Haard N.F. Degradation of proteoglycans in the skeletal muscle of Pacific rockfish (Sebastes sp.) during ice storage. J. Muscle Foods 3 (1992) 103-121
    • (1992) J. Muscle Foods , vol.3 , pp. 103-121
    • Kim, K.1    Haard, N.F.2
  • 15
    • 0001071205 scopus 로고    scopus 로고
    • Possible implication of metalloproteinases in post-mortem tenderization of fish muscle
    • Kubota M., Kinoshita M., Takeuchi K., Kubota S., Toyohara H., and Sakaguchi M. Possible implication of metalloproteinases in post-mortem tenderization of fish muscle. Fish. Sci. 67 5 (2001) 965-968
    • (2001) Fish. Sci. , vol.67 , Issue.5 , pp. 965-968
    • Kubota, M.1    Kinoshita, M.2    Takeuchi, K.3    Kubota, S.4    Toyohara, H.5    Sakaguchi, M.6
  • 16
    • 0037409612 scopus 로고    scopus 로고
    • In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L.): effects of cathepsins B, D and L
    • Ladrat C., Verrez-Bagnis V., Noël J., and Fleurence J. In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L.): effects of cathepsins B, D and L. Food Chem. 81 (2003) 517-525
    • (2003) Food Chem. , vol.81 , pp. 517-525
    • Ladrat, C.1    Verrez-Bagnis, V.2    Noël, J.3    Fleurence, J.4
  • 19
    • 33745210338 scopus 로고    scopus 로고
    • Breakdown of intramuscular connective tissue in cod (Gadus morhua L.) and spotted wolfish (Anarhichas minor O.) related to gaping
    • Ofstad R., Olsen R.L., Taylor R., and Hannesson K.O. Breakdown of intramuscular connective tissue in cod (Gadus morhua L.) and spotted wolfish (Anarhichas minor O.) related to gaping. LWT 39 (2006) 1143-1154
    • (2006) LWT , vol.39 , pp. 1143-1154
    • Ofstad, R.1    Olsen, R.L.2    Taylor, R.3    Hannesson, K.O.4
  • 20
    • 0029828561 scopus 로고    scopus 로고
    • Post mortem release of fish white muscle alpha-actinin as a marker of disorganization
    • Papa I., Alvarez C., Verrez-Bagnis V., Fleurence J., and Benyamin Y. Post mortem release of fish white muscle alpha-actinin as a marker of disorganization. J. Sci. Food Agric. 72 (1996) 63-70
    • (1996) J. Sci. Food Agric. , vol.72 , pp. 63-70
    • Papa, I.1    Alvarez, C.2    Verrez-Bagnis, V.3    Fleurence, J.4    Benyamin, Y.5
  • 21
    • 0030656229 scopus 로고    scopus 로고
    • Dystrophin cleavage and sarcolemma detachment are early post mortem changes on Bass (Dicentrarchus labrax) white muscle
    • Papa I., Taylor R.G., Astier C., Ventre F., Lebart M.C., Roustan C., Ouali A., and Benyamin Y. Dystrophin cleavage and sarcolemma detachment are early post mortem changes on Bass (Dicentrarchus labrax) white muscle. J. Food Sci. 62 (1997) 917-921
    • (1997) J. Food Sci. , vol.62 , pp. 917-921
    • Papa, I.1    Taylor, R.G.2    Astier, C.3    Ventre, F.4    Lebart, M.C.5    Roustan, C.6    Ouali, A.7    Benyamin, Y.8
  • 22
    • 0000833688 scopus 로고
    • Type V collagen in trout (Salmo gairdneri) muscle and its solubility change during chilled storage of muscle
    • Sato K., Ohashi C., Ohtsuki K., and Kawabata M. Type V collagen in trout (Salmo gairdneri) muscle and its solubility change during chilled storage of muscle. J. Agric. Food Chem. 39 (1991) 1222-1225
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 1222-1225
    • Sato, K.1    Ohashi, C.2    Ohtsuki, K.3    Kawabata, M.4
  • 24
    • 0034997402 scopus 로고    scopus 로고
    • Fiber type-specific expression of major proteolytic systems in fast- to slow-transforming rabbit muscle
    • Sultan K.R., Dittrich B.T., Leisner E., Paul N., and Pette D. Fiber type-specific expression of major proteolytic systems in fast- to slow-transforming rabbit muscle. Am. J. Physiol. Cell Physiol. 280 (2001) 239-247
    • (2001) Am. J. Physiol. Cell Physiol. , vol.280 , pp. 239-247
    • Sultan, K.R.1    Dittrich, B.T.2    Leisner, E.3    Paul, N.4    Pette, D.5
  • 26
    • 0036691070 scopus 로고    scopus 로고
    • Salmon fillet texture is determined by myofiber-myofiber and myofiber-myocommata attachment
    • Taylor R.G., Fjaera S.O., and Skjervold P.O. Salmon fillet texture is determined by myofiber-myofiber and myofiber-myocommata attachment. Food Chem. Toxicol. 67 (2002) 2067-2071
    • (2002) Food Chem. Toxicol. , vol.67 , pp. 2067-2071
    • Taylor, R.G.1    Fjaera, S.O.2    Skjervold, P.O.3
  • 28
    • 85008099141 scopus 로고
    • Postmortem changes in alpha-actinin and connectin in carp and rainbow trout muscles
    • Tsuchiya H., Kita S., and Seki N. Postmortem changes in alpha-actinin and connectin in carp and rainbow trout muscles. Nippon Suisan Gakkaishi 58 (1992) 793-798
    • (1992) Nippon Suisan Gakkaishi , vol.58 , pp. 793-798
    • Tsuchiya, H.1    Kita, S.2    Seki, N.3
  • 29
    • 0027992766 scopus 로고
    • Regulation of proteolytic activity in tissues
    • Twining S.S. Regulation of proteolytic activity in tissues. Crit. Rev. Biochem. Mol. Biol. 29 (1994) 315-383
    • (1994) Crit. Rev. Biochem. Mol. Biol. , vol.29 , pp. 315-383
    • Twining, S.S.1
  • 31
    • 0036721076 scopus 로고    scopus 로고
    • In vitro proteolysis of myofibrillar and sarcoplasmic proteins of European sea bass (Dicentrarchus labrax L) by an endogenous m-calpain
    • Verrez-Bagnis V., Ladrat C., Noëlle J., and Fleurence J. In vitro proteolysis of myofibrillar and sarcoplasmic proteins of European sea bass (Dicentrarchus labrax L) by an endogenous m-calpain. J. Sci. Food Agric. 82 (2002) 1256-1262
    • (2002) J. Sci. Food Agric. , vol.82 , pp. 1256-1262
    • Verrez-Bagnis, V.1    Ladrat, C.2    Noëlle, J.3    Fleurence, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.