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Volumn 310, Issue 1-2, 2010, Pages 213-220

Fillet texture and protease activities in different families of farmed Atlantic salmon (Salmo salar L.)

Author keywords

Calpains; Calpastatins; Cathepsins; Firmness; Fish quality

Indexed keywords

ENZYME ACTIVITY; GENETIC VARIATION; MUSCLE; PROTEIN; SALMONID CULTURE; TEXTURE;

EID: 78649706405     PISSN: 00448486     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.aquaculture.2010.10.008     Document Type: Article
Times cited : (48)

References (65)
  • 1
    • 84986776508 scopus 로고
    • Postmortem tenderization of Rainbow-Trout (Oncorhynchus mykiss) muscle caused by gradual disintegration of the extracellular-matrix structure
    • Ando M., Toyohara H., Shimizu Y., Sakaguchi M. Postmortem tenderization of Rainbow-Trout (Oncorhynchus mykiss) muscle caused by gradual disintegration of the extracellular-matrix structure. J. Sci. Food Agric. 1991, 55:589-597.
    • (1991) J. Sci. Food Agric. , vol.55 , pp. 589-597
    • Ando, M.1    Toyohara, H.2    Shimizu, Y.3    Sakaguchi, M.4
  • 2
    • 0000903338 scopus 로고
    • Postmortem tenderization of Rainbow-Trout muscle caused by the desintegration of collagen-fibers in the pericellular connective-tissue
    • Ando M., Toyohara H., Sakaguchi M. Postmortem tenderization of Rainbow-Trout muscle caused by the desintegration of collagen-fibers in the pericellular connective-tissue. Nippon Suisan Gakkaishi 1992, 58:567-570.
    • (1992) Nippon Suisan Gakkaishi , vol.58 , pp. 567-570
    • Ando, M.1    Toyohara, H.2    Sakaguchi, M.3
  • 3
    • 0034846451 scopus 로고    scopus 로고
    • Influence of death struggle on the structural changes in chub mackerel muscle during chilled storage
    • Ando M., Joka M., Mochizuki S., Satoh K.I., Tsukamasa Y., Makinodan Y. Influence of death struggle on the structural changes in chub mackerel muscle during chilled storage. Fish. Sci. 2001, 67:744-751.
    • (2001) Fish. Sci. , vol.67 , pp. 744-751
    • Ando, M.1    Joka, M.2    Mochizuki, S.3    Satoh, K.I.4    Tsukamasa, Y.5    Makinodan, Y.6
  • 4
    • 33846578689 scopus 로고    scopus 로고
    • Pre-slaughter crowding stress and killing procedures affecting quality and welfare in sea bass (Dicentrarchus labrax) and sea bream (Sparus aurata)
    • Bagni M., Civitareale C., Priori A., Ballerini A., Finola M., Brambilla G., Marino G. Pre-slaughter crowding stress and killing procedures affecting quality and welfare in sea bass (Dicentrarchus labrax) and sea bream (Sparus aurata). Aquaculture 2007, 263:52-60.
    • (2007) Aquaculture , vol.263 , pp. 52-60
    • Bagni, M.1    Civitareale, C.2    Priori, A.3    Ballerini, A.4    Finola, M.5    Brambilla, G.6    Marino, G.7
  • 5
    • 60249091249 scopus 로고    scopus 로고
    • Atlantic salmon (Salmo salar) muscle structure integrity and lysosomal cathepsins B and L influenced by dietary n-6 and n-3 fatty acids
    • Bahuaud D., Østbye T.K., Torstensen B.E., Rørå M.B., Ofstad R., Veiseth E., Thomassen M.S., Ruyter B. Atlantic salmon (Salmo salar) muscle structure integrity and lysosomal cathepsins B and L influenced by dietary n-6 and n-3 fatty acids. Food Chemistry 2009, 114(4):1421-1432.
    • (2009) Food Chemistry , vol.114 , Issue.4 , pp. 1421-1432
    • Bahuaud, D.1    Østbye, T.K.2    Torstensen, B.E.3    Rørå, M.B.4    Ofstad, R.5    Veiseth, E.6    Thomassen, M.S.7    Ruyter, B.8
  • 6
    • 69349105797 scopus 로고    scopus 로고
    • Muscle structure responses and lysosomal cathepsins B and L in farmed Atlantic salmon (Salmo salar L.) pre- and post-rigor fillets exposed to short and long-term crowding stress
    • Bahuaud D., Mørkøre T., Østbye T.K., Veiseth-Kent E., Thomassen M.S., Ofstad R. Muscle structure responses and lysosomal cathepsins B and L in farmed Atlantic salmon (Salmo salar L.) pre- and post-rigor fillets exposed to short and long-term crowding stress. Food Chemistry 2010, 118(3):602-615.
    • (2010) Food Chemistry , vol.118 , Issue.3 , pp. 602-615
    • Bahuaud, D.1    Mørkøre, T.2    Østbye, T.K.3    Veiseth-Kent, E.4    Thomassen, M.S.5    Ofstad, R.6
  • 8
    • 29844453940 scopus 로고    scopus 로고
    • Textural properties of raw Atlantic salmon (Salmo salar) at three points along the fillet, determined by different methods
    • Casas C., Martinez O., Guillen M.D., Pin C., Salmeron J. Textural properties of raw Atlantic salmon (Salmo salar) at three points along the fillet, determined by different methods. Food Control 2006, 17:511-515.
    • (2006) Food Control , vol.17 , pp. 511-515
    • Casas, C.1    Martinez, O.2    Guillen, M.D.3    Pin, C.4    Salmeron, J.5
  • 11
    • 0017101433 scopus 로고
    • 2+ activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme
    • 2+ activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme. Biochemistry 1976, 15:2159-2167.
    • (1976) Biochemistry , vol.15 , pp. 2159-2167
    • Dayton, W.R.1    Reville, W.J.2    Goll, D.E.3    Stormer, M.H.4
  • 12
    • 0029084425 scopus 로고
    • Inhibition of chondrocyte cathepsin B and L activities by insulin-like growth factor-II (IGF-II) and its Ser29 variant in vitro: possible role of the mannose 6-phosphate/IGF-II receptor
    • De Ceuninck F., Poiraudeau S., Pagano M., Tsagris L., Blanchard O., Willeput J., Corvol M. Inhibition of chondrocyte cathepsin B and L activities by insulin-like growth factor-II (IGF-II) and its Ser29 variant in vitro: possible role of the mannose 6-phosphate/IGF-II receptor. Molecular and Cellular Endocrinology 1995, 113:205-213.
    • (1995) Molecular and Cellular Endocrinology , vol.113 , pp. 205-213
    • De Ceuninck, F.1    Poiraudeau, S.2    Pagano, M.3    Tsagris, L.4    Blanchard, O.5    Willeput, J.6    Corvol, M.7
  • 13
    • 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., 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 Chemistry 2004, 84:441-446.
    • (2004) Food Chemistry , vol.84 , pp. 441-446
    • Delbarre-Ladrat, C.1    Verrez-Bagnis, V.2    Noël, J.3    Fleurence, J.4
  • 14
    • 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., Noel J., Fleurence J. Relative contribution of calpain and cathepsins to protein degradation in muscle of sea bass (Dicentrarchus labrax L.). Food Chemistry 2004, 88:389-395.
    • (2004) Food Chemistry , vol.88 , pp. 389-395
    • Delbarre-Ladrat, C.1    Verrez-Bagnis, V.2    Noel, J.3    Fleurence, J.4
  • 15
    • 0032212702 scopus 로고    scopus 로고
    • Starvation prior to slaughter in Atlantic salmon (Salmo salar). II. White muscle composition and evaluation of freshness, texture and colour characteristics in raw and cooked fillets
    • Einen O., Thomassen M.S. Starvation prior to slaughter in Atlantic salmon (Salmo salar). II. White muscle composition and evaluation of freshness, texture and colour characteristics in raw and cooked fillets. Aquaculture 1998, 169:37-53.
    • (1998) Aquaculture , vol.169 , pp. 37-53
    • Einen, O.1    Thomassen, M.S.2
  • 17
    • 32344452656 scopus 로고    scopus 로고
    • Live chilling of Atlantic salmon (Salmo salar) combined with mild carbon dioxide anaesthesia. I. Establishing a method for large-scale processing of farmed fish
    • Erikson U., Hultmann L., Steen J.E. Live chilling of Atlantic salmon (Salmo salar) combined with mild carbon dioxide anaesthesia. I. Establishing a method for large-scale processing of farmed fish. Aquaculture 2006, 252:183-198.
    • (2006) Aquaculture , vol.252 , pp. 183-198
    • Erikson, U.1    Hultmann, L.2    Steen, J.E.3
  • 18
    • 4944239112 scopus 로고    scopus 로고
    • Interactions between ice storage time, collagen composition, gaping and textural properties in farmed salmon muscle harvested at different times of the year
    • Espe M., Ruohonen K., Bjornevik M., Froyland L., Nortvedt R., Kiessling A. Interactions between ice storage time, collagen composition, gaping and textural properties in farmed salmon muscle harvested at different times of the year. Aquaculture 2004, 240:489-504.
    • (2004) Aquaculture , vol.240 , pp. 489-504
    • Espe, M.1    Ruohonen, K.2    Bjornevik, M.3    Froyland, L.4    Nortvedt, R.5    Kiessling, A.6
  • 19
    • 0141920735 scopus 로고    scopus 로고
    • Effects of rearing temperature and strain on sensory characteristics, texture, colour and fat of Arctic charr (Salvelinus alpinus)
    • Ginés R., Valdimarsdottir T., Sveinsdottir K., Thorarensen H. Effects of rearing temperature and strain on sensory characteristics, texture, colour and fat of Arctic charr (Salvelinus alpinus). Food Quality and Preference 2004, 15:177-185.
    • (2004) Food Quality and Preference , vol.15 , pp. 177-185
    • Ginés, R.1    Valdimarsdottir, T.2    Sveinsdottir, K.3    Thorarensen, H.4
  • 20
    • 0033955861 scopus 로고    scopus 로고
    • Genetic improvement of cold-water fish species
    • Gjedrem T. Genetic improvement of cold-water fish species. Aquaculture Research 2000, 31:25-33.
    • (2000) Aquaculture Research , vol.31 , pp. 25-33
    • Gjedrem, T.1
  • 21
    • 56149116038 scopus 로고    scopus 로고
    • Contribution of cathepsins B, L and D to muscle protein profiles correlated with texture in rainbow trout (Oncorhynchus mykiss)
    • Godiksen H., Morzel M., Hyldig G., Jessen F. Contribution of cathepsins B, L and D to muscle protein profiles correlated with texture in rainbow trout (Oncorhynchus mykiss). Food Chemistry 2009, 113:889-896.
    • (2009) Food Chemistry , vol.113 , pp. 889-896
    • Godiksen, H.1    Morzel, M.2    Hyldig, G.3    Jessen, F.4
  • 25
    • 85029923978 scopus 로고    scopus 로고
    • Endogenous proteolytic enzymes-studies of their impact on fish muscle proteins and texture, Department of Biotechnology
    • Hultmann L. Endogenous proteolytic enzymes-studies of their impact on fish muscle proteins and texture, Department of Biotechnology. Faculty of Natural Sciences and Technology, Trondheim, Norway 2003.
    • (2003) Faculty of Natural Sciences and Technology, Trondheim, Norway
    • Hultmann, L.1
  • 26
    • 1942446324 scopus 로고    scopus 로고
    • Iced storage of Atlantic salmon (Salmo salar)-effects on endogenous enzymes and their impact on muscle proteins and texture
    • Hultmann L., Rustad T. Iced storage of Atlantic salmon (Salmo salar)-effects on endogenous enzymes and their impact on muscle proteins and texture. Food Chemistry 2004, 87:31-41.
    • (2004) Food Chemistry , vol.87 , pp. 31-41
    • Hultmann, L.1    Rustad, T.2
  • 27
    • 34248999164 scopus 로고    scopus 로고
    • Effects of temperature abuse on textural properties and proteolytic activities during post mortem iced storage of farmed Atlantic cod (Gadus morhua)
    • Hultmann L., Rustad T. Effects of temperature abuse on textural properties and proteolytic activities during post mortem iced storage of farmed Atlantic cod (Gadus morhua). Food Chemistry 2007, 104:1687-1697.
    • (2007) Food Chemistry , vol.104 , pp. 1687-1697
    • Hultmann, L.1    Rustad, T.2
  • 28
    • 27344460458 scopus 로고    scopus 로고
    • Alterations in fillet fatty acid profile and flesh quality in gilthead seabream (Sparus aurata) fed vegetable oils for a long term period. Recovery of fatty acid profiles by fish oil feeding
    • Izquierdo M.S., Montero D., Robaina L., Caballero M.J., Rosenlund G., Gines R. Alterations in fillet fatty acid profile and flesh quality in gilthead seabream (Sparus aurata) fed vegetable oils for a long term period. Recovery of fatty acid profiles by fish oil feeding. Aquaculture 2005, 250:431-444.
    • (2005) Aquaculture , vol.250 , pp. 431-444
    • Izquierdo, M.S.1    Montero, D.2    Robaina, L.3    Caballero, M.J.4    Rosenlund, G.5    Gines, R.6
  • 33
    • 0020512030 scopus 로고
    • Activity of lysosomal cysteine proteinase during differentiation of rat skeletal-muscle
    • Kirschke H., Wood L., Roisen F.J., Bird J.W.C. Activity of lysosomal cysteine proteinase during differentiation of rat skeletal-muscle. Biochemical Journal 1983, 214:871-877.
    • (1983) Biochemical Journal , vol.214 , pp. 871-877
    • Kirschke, H.1    Wood, L.2    Roisen, F.J.3    Bird, J.W.C.4
  • 34
    • 0026591107 scopus 로고
    • 2+-dependent proteases (calpains) in post mortem proteolysis and meat tenderness
    • 2+-dependent proteases (calpains) in post mortem proteolysis and meat tenderness. Biochimie 1992, 74:239-245.
    • (1992) Biochimie , vol.74 , pp. 239-245
    • Koohmaraie, M.1
  • 35
    • 0030305245 scopus 로고    scopus 로고
    • Biochemical factors regulating the toughening and tenderization processes of meat
    • Koohmaraie M. Biochemical factors regulating the toughening and tenderization processes of meat. Meat Science 1996, 43:193-201.
    • (1996) Meat Science , vol.43 , pp. 193-201
    • Koohmaraie, M.1
  • 36
    • 33745648075 scopus 로고    scopus 로고
    • Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system
    • Koohmaraie M., Geesink G.H. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Science 2006, 74:34-43.
    • (2006) Meat Science , vol.74 , pp. 34-43
    • Koohmaraie, M.1    Geesink, G.H.2
  • 38
    • 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., Noel J., 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 Chemistry 2003, 81:517-525.
    • (2003) Food Chemistry , vol.81 , pp. 517-525
    • Ladrat, C.1    Verrez-Bagnis, V.2    Noel, J.3    Fleurence, J.4
  • 40
    • 0027615958 scopus 로고
    • Meat tenderness and the calpain proteolytic system in longissimus muscle of young bulls and steers
    • Morgan J.B., Wheeler T.L., Koohmaraie M., Savell J.W., Crouse J.D. Meat tenderness and the calpain proteolytic system in longissimus muscle of young bulls and steers. Journal of Animal Science 1993, 71:1471-1476.
    • (1993) Journal of Animal Science , vol.71 , pp. 1471-1476
    • Morgan, J.B.1    Wheeler, T.L.2    Koohmaraie, M.3    Savell, J.W.4    Crouse, J.D.5
  • 42
    • 0037851838 scopus 로고    scopus 로고
    • Relating sensory and instrumental texture analyses of Atlantic salmon
    • Mørkøre T., Einen O. Relating sensory and instrumental texture analyses of Atlantic salmon. Journal of Food Science 2003, 68:1492-1497.
    • (2003) Journal of Food Science , vol.68 , pp. 1492-1497
    • Mørkøre, T.1    Einen, O.2
  • 43
    • 0842307816 scopus 로고    scopus 로고
    • Seasonal variations in growth, feed utilisation and product quality of farmed Atlantic salmon (Salmo salar) transferred to seawater as 0+smolts or 1+smolts
    • Mørkøre T., Rørvik K.A. Seasonal variations in growth, feed utilisation and product quality of farmed Atlantic salmon (Salmo salar) transferred to seawater as 0+smolts or 1+smolts. Aquaculture 2001, 199:145-157.
    • (2001) Aquaculture , vol.199 , pp. 145-157
    • Mørkøre, T.1    Rørvik, K.A.2
  • 44
    • 42749090617 scopus 로고    scopus 로고
    • Impact of starvation and handling stress on rigor development and quality of Atlantic salmon (Salmon salar L.)
    • Mørkøre T., Mazo T.P.I., Tahirovic V., Einen O. Impact of starvation and handling stress on rigor development and quality of Atlantic salmon (Salmon salar L.). Aquaculture 2008, 277:231-238.
    • (2008) Aquaculture , vol.277 , pp. 231-238
    • Mørkøre, T.1    Mazo, T.P.I.2    Tahirovic, V.3    Einen, O.4
  • 45
    • 39149091343 scopus 로고    scopus 로고
    • Genetic parameters of production traits in Atlantic salmon (Salmo salar)
    • Powell J., White I., Guy D., Brotherstone S. Genetic parameters of production traits in Atlantic salmon (Salmo salar). Aquaculture 2008, 274:225-231.
    • (2008) Aquaculture , vol.274 , pp. 225-231
    • Powell, J.1    White, I.2    Guy, D.3    Brotherstone, S.4
  • 47
    • 0029048989 scopus 로고
    • Casein zymography: a method to study μ-calpain, m-calpain, and their inhibitory agents
    • Raser K.J., Posner A., Wang K.W. Casein zymography: a method to study μ-calpain, m-calpain, and their inhibitory agents. Archives of Biochemistry and biophysics 1995, 319(1):211-216.
    • (1995) Archives of Biochemistry and biophysics , vol.319 , Issue.1 , pp. 211-216
    • Raser, K.J.1    Posner, A.2    Wang, K.W.3
  • 48
    • 0034772117 scopus 로고    scopus 로고
    • Quality of farmed salmonids with emphasis on proximate composition, yield and sensory characteristics
    • Rasmussen R.S. Quality of farmed salmonids with emphasis on proximate composition, yield and sensory characteristics. Aquaculture Research 2001, 32:767-786.
    • (2001) Aquaculture Research , vol.32 , pp. 767-786
    • Rasmussen, R.S.1
  • 49
    • 13844276995 scopus 로고    scopus 로고
    • Isolation and characterization of calpains from rainbow trout muscle and their role in texture development
    • Salem M., Kenney P.B., Killefer J., Nath J. Isolation and characterization of calpains from rainbow trout muscle and their role in texture development. Journal of Muscle Foods 2004, 15:245-255.
    • (2004) Journal of Muscle Foods , vol.15 , pp. 245-255
    • Salem, M.1    Kenney, P.B.2    Killefer, J.3    Nath, J.4
  • 52
    • 0028417554 scopus 로고
    • Heritabilities and phenotypic and genetic correlations for bovine postrigor calpastatin activity, intramuscular fat content, Warner-Bratzler shear force, retail product yield, and growth rate
    • Shackelford S.D., Koohmaraie M., Cundiff L.V., Gregory K.E., Rohrer G.A., Savell J.W. Heritabilities and phenotypic and genetic correlations for bovine postrigor calpastatin activity, intramuscular fat content, Warner-Bratzler shear force, retail product yield, and growth rate. Journal of Animal Science 1994, 72:857-863.
    • (1994) Journal of Animal Science , vol.72 , pp. 857-863
    • Shackelford, S.D.1    Koohmaraie, M.2    Cundiff, L.V.3    Gregory, K.E.4    Rohrer, G.A.5    Savell, J.W.6
  • 53
    • 0035862805 scopus 로고    scopus 로고
    • Live-chilling and crowding stress before slaughter of Atlantic salmon (Salmo salar)
    • Skjervold P.O., Fjæra S.O., Ostby P.B., Einen O. Live-chilling and crowding stress before slaughter of Atlantic salmon (Salmo salar). Aquaculture 2001, 192:265-280.
    • (2001) Aquaculture , vol.192 , pp. 265-280
    • Skjervold, P.O.1    Fjæra, S.O.2    Ostby, P.B.3    Einen, O.4
  • 57
    • 0036691070 scopus 로고    scopus 로고
    • Salmon fillet texture is determined by myofiber-myofiber and myofiber-myocommata attachment
    • Taylor R.G., Fjæra S.O., Skjervold P.O. Salmon fillet texture is determined by myofiber-myofiber and myofiber-myocommata attachment. Journal of Food Science 2002, 67:2067-2071.
    • (2002) Journal of Food Science , vol.67 , pp. 2067-2071
    • Taylor, R.G.1    Fjæra, S.O.2    Skjervold, P.O.3
  • 58
    • 0034653992 scopus 로고    scopus 로고
    • A BODIPY fluorescent microplate assay for measuring activity of calpains and other proteinases
    • Thompson V.F., Saldaña S., Cong J.Y., Goll D.E. A BODIPY fluorescent microplate assay for measuring activity of calpains and other proteinases. Analytic Biochemistry 2000, 279:170-178.
    • (2000) Analytic Biochemistry , vol.279 , pp. 170-178
    • Thompson, V.F.1    Saldaña, S.2    Cong, J.Y.3    Goll, D.E.4
  • 59
    • 0035545539 scopus 로고    scopus 로고
    • Effect of extraction buffer on estimating calpain and calpastatin activity in postmortem ovine muscle
    • Veiseth E., Koohmaraie M. Effect of extraction buffer on estimating calpain and calpastatin activity in postmortem ovine muscle. Meat Science 2001, 57:325-329.
    • (2001) Meat Science , vol.57 , pp. 325-329
    • Veiseth, E.1    Koohmaraie, M.2
  • 61
    • 4043126640 scopus 로고    scopus 로고
    • Factors regulating lamb longissimus tenderness are affected by age at slaughter
    • Veiseth E., Shackelford S.D., Wheeler T.L., Koohmaraie M. Factors regulating lamb longissimus tenderness are affected by age at slaughter. Meat Science 2004, 68:635-640.
    • (2004) Meat Science , vol.68 , pp. 635-640
    • Veiseth, E.1    Shackelford, S.D.2    Wheeler, T.L.3    Koohmaraie, M.4
  • 62
    • 0034170872 scopus 로고    scopus 로고
    • Evaluation of calpastatin activity measured in ante- and postmortem muscle from half-sib bulls and steers
    • Woodward B.W., DeNise S.K., Marchello J.A. Evaluation of calpastatin activity measured in ante- and postmortem muscle from half-sib bulls and steers. Journal of Animal Science 2000, 78:804-809.
    • (2000) Journal of Animal Science , vol.78 , pp. 804-809
    • Woodward, B.W.1    DeNise, S.K.2    Marchello, J.A.3
  • 63
    • 85008070248 scopus 로고
    • Participation of cathepsin L into extensive softening of the muscle of chum salmon caught during spawning migration
    • Yamashita M., Konagaya S. Participation of cathepsin L into extensive softening of the muscle of chum salmon caught during spawning migration. Nippon Suisan Gakkaishi 1990, 56:1271-1277.
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 1271-1277
    • Yamashita, M.1    Konagaya, S.2
  • 64
    • 85010180489 scopus 로고
    • Hydrolytic action of salmon cathepsin-B and Cathepsin-L to muscle structural proteins in respect of muscle softening
    • Yamashita M., Konagaya S. Hydrolytic action of salmon cathepsin-B and Cathepsin-L to muscle structural proteins in respect of muscle softening. Nippon Suisan Gakkaishi 1991, 57:1917-1922.
    • (1991) Nippon Suisan Gakkaishi , vol.57 , pp. 1917-1922
    • Yamashita, M.1    Konagaya, S.2
  • 65
    • 15344345075 scopus 로고    scopus 로고
    • Time-related changes in cathepsin B and L activities during processing of Jinhua ham as a function of pH, salt and temperature
    • Zhao G.M., Zhou G.H., Wang Y.L., Xu X.L., Huan Y.J., Wu J.Q. Time-related changes in cathepsin B and L activities during processing of Jinhua ham as a function of pH, salt and temperature. Meat Science 2005, 70:381-388.
    • (2005) Meat Science , vol.70 , pp. 381-388
    • Zhao, G.M.1    Zhou, G.H.2    Wang, Y.L.3    Xu, X.L.4    Huan, Y.J.5    Wu, J.Q.6


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