메뉴 건너뛰기




Volumn 124, Issue 1, 2011, Pages 254-261

Isolation, characterisation and stability of myoglobin from Eastern little tuna (Euthynnus affinis) dark muscle

Author keywords

Characterisation; Eastern little tuna; Metmyoglobin; Myoglobin; Oxymyoglobin; Stability

Indexed keywords

CHARACTERISATION; EASTERN LITTLE TUNA; METMYOGLOBIN; MYOGLOBIN; OXYMYOGLOBIN;

EID: 77955276845     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2010.06.028     Document Type: Article
Times cited : (48)

References (36)
  • 1
    • 33745462677 scopus 로고    scopus 로고
    • Characterisation of myoglobin from sardine (Sardinella gibbosa) dark muscle
    • Chaijan M., Benjakul S., Visessanguan W., Faustman C. Characterisation of myoglobin from sardine (Sardinella gibbosa) dark muscle. Food Chemistry 2007, 100:156-164.
    • (2007) Food Chemistry , vol.100 , pp. 156-164
    • Chaijan, M.1    Benjakul, S.2    Visessanguan, W.3    Faustman, C.4
  • 2
    • 0034656968 scopus 로고    scopus 로고
    • Separation and quality of fish oil from precooked and non-precooked tuna heads
    • Chantachum S., Benjakul S., Sriwirat N. Separation and quality of fish oil from precooked and non-precooked tuna heads. Food Chemistry 2000, 69:289-294.
    • (2000) Food Chemistry , vol.69 , pp. 289-294
    • Chantachum, S.1    Benjakul, S.2    Sriwirat, N.3
  • 3
    • 0011762658 scopus 로고    scopus 로고
    • Studies on thermal denaturation of fish myoglobins using differential scanning calorimetry, circular dichroism and tryptophan fluorescence
    • Chanthai S., Ogawa M., Tamiya T., Tsuchiya T. Studies on thermal denaturation of fish myoglobins using differential scanning calorimetry, circular dichroism and tryptophan fluorescence. Fisheries Science 1996, 62:927-932.
    • (1996) Fisheries Science , vol.62 , pp. 927-932
    • Chanthai, S.1    Ogawa, M.2    Tamiya, T.3    Tsuchiya, T.4
  • 4
    • 0035533770 scopus 로고    scopus 로고
    • Studies on the physicochemical properties of milkfish myoglobin
    • Chen W.L., Chow C.J. Studies on the physicochemical properties of milkfish myoglobin. Journal of Food Biochemistry 2001, 25:157-174.
    • (2001) Journal of Food Biochemistry , vol.25 , pp. 157-174
    • Chen, W.L.1    Chow, C.J.2
  • 5
    • 2442586757 scopus 로고    scopus 로고
    • Thermal stability and denaturation rate of myoglobin from various species of fish
    • Chen L.C., Lin S.B., Chen H.H. Thermal stability and denaturation rate of myoglobin from various species of fish. Fisheries Science 2004, 70:293-298.
    • (2004) Fisheries Science , vol.70 , pp. 293-298
    • Chen, L.C.1    Lin, S.B.2    Chen, H.H.3
  • 6
    • 3042665289 scopus 로고    scopus 로고
    • Effect of frozen temperature on autoxidation and aggregation of bluefin tuna myoglobin in solution
    • Chow C.J., Ochiai Y., Watabe S. Effect of frozen temperature on autoxidation and aggregation of bluefin tuna myoglobin in solution. Journal of Food Biochemistry 2004, 28:123-134.
    • (2004) Journal of Food Biochemistry , vol.28 , pp. 123-134
    • Chow, C.J.1    Ochiai, Y.2    Watabe, S.3
  • 9
    • 33745639687 scopus 로고    scopus 로고
    • The influence of storage conditions of tuna viscera before fermentation on the chemical, physical and microbiological changes in fish sauce during fermentation
    • Dissaraphong S., Benjakul S., Visessanguan W., Kishimura H. The influence of storage conditions of tuna viscera before fermentation on the chemical, physical and microbiological changes in fish sauce during fermentation. Bioresource Technology 2006, 97:2032-2040.
    • (2006) Bioresource Technology , vol.97 , pp. 2032-2040
    • Dissaraphong, S.1    Benjakul, S.2    Visessanguan, W.3    Kishimura, H.4
  • 10
    • 84930481689 scopus 로고
    • The biochemical basis for discoloration in fresh meat: A review
    • Faustman C., Cassens R.G. The biochemical basis for discoloration in fresh meat: A review. Journal of Muscle Foods 1990, 1:217-243.
    • (1990) Journal of Muscle Foods , vol.1 , pp. 217-243
    • Faustman, C.1    Cassens, R.G.2
  • 11
    • 77955269680 scopus 로고    scopus 로고
    • Fisheries Foreign Affairs Division. Statistics on fishery production, 2007. Retrieved March 19, from Ministry of Agriculture and Co-operatives, Web site: .
    • Fisheries Foreign Affairs Division (2007). Statistics on fishery production, 2007. Retrieved March 19, from Ministry of Agriculture and Co-operatives, Web site: http://www.fisheries.go.th.
    • (2007)
  • 12
    • 0017112522 scopus 로고
    • Yellowfin tuna (Thunnus albacares) myoglobin: Characterization and comparative stability
    • Fosmire G.J., Brown W.D. Yellowfin tuna (Thunnus albacares) myoglobin: Characterization and comparative stability. Comparative Biochemistry and Physiology 1976, 55B:293-299.
    • (1976) Comparative Biochemistry and Physiology , vol.55 B , pp. 293-299
    • Fosmire, G.J.1    Brown, W.D.2
  • 15
    • 0001748740 scopus 로고    scopus 로고
    • Effect of heat denaturation on the pro-oxidative activity of metmyoglobin in linoleic acid emulsions
    • Kristensen L., Andersen H.J. Effect of heat denaturation on the pro-oxidative activity of metmyoglobin in linoleic acid emulsions. Journal of Agricultural and Food Chemistry 1997, 45:7-13.
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 7-13
    • Kristensen, L.1    Andersen, H.J.2
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0035612494 scopus 로고    scopus 로고
    • Contribution of pigment content, myoglobin forms and internal reflectance to the colour of pork loin and ham from pure breed pigs
    • Lindahl G., Lundstrom K., Tornberg E. Contribution of pigment content, myoglobin forms and internal reflectance to the colour of pork loin and ham from pure breed pigs. Meat Science 2001, 59:141-151.
    • (2001) Meat Science , vol.59 , pp. 141-151
    • Lindahl, G.1    Lundstrom, K.2    Tornberg, E.3
  • 18
    • 0035937761 scopus 로고    scopus 로고
    • Waterproofing the heme pocket. Role of proximal amino acid side chains in preventing hemin loss from myoglobin
    • Liong E.C., Dou Y., Scott E.E., Olson J.S., Phillips G.N. Waterproofing the heme pocket. Role of proximal amino acid side chains in preventing hemin loss from myoglobin. Journal of Biological Chemistry 2001, 276:9093-9100.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 9093-9100
    • Liong, E.C.1    Dou, Y.2    Scott, E.E.3    Olson, J.S.4    Phillips, G.N.5
  • 23
    • 0000697994 scopus 로고
    • Autoxidation of purified myoglobin from two bovine muscles
    • Renerre M., Anton M., Gatellier P. Autoxidation of purified myoglobin from two bovine muscles. Meat Science 1992, 32:331-342.
    • (1992) Meat Science , vol.32 , pp. 331-342
    • Renerre, M.1    Anton, M.2    Gatellier, P.3
  • 24
    • 84987265506 scopus 로고
    • Porcine and ovine myoglobin: Isolation, purification, characterization and stability
    • Satterlee L.D., Zachariah N.Y. Porcine and ovine myoglobin: Isolation, purification, characterization and stability. Journal of Food Science 1972, 37:909-912.
    • (1972) Journal of Food Science , vol.37 , pp. 909-912
    • Satterlee, L.D.1    Zachariah, N.Y.2
  • 28
    • 33748806801 scopus 로고    scopus 로고
    • A rapid spectroscopic method to detect the fraudulent treatment of tuna fish with carbon monoxide
    • Smulevich G., Droghetti E., Focardi C., Coletta M., Ciaccio C., Nocentini M. A rapid spectroscopic method to detect the fraudulent treatment of tuna fish with carbon monoxide. Food Chemistry 2007, 101:1071-1077.
    • (2007) Food Chemistry , vol.101 , pp. 1071-1077
    • Smulevich, G.1    Droghetti, E.2    Focardi, C.3    Coletta, M.4    Ciaccio, C.5    Nocentini, M.6
  • 29
    • 25844525770 scopus 로고    scopus 로고
    • Lipid oxidations in ordinary and dark muscles of fish: Influences on rancid off-odor development and color darkening of yellowtail flesh during ice storage
    • Sohn J.H., Taki Y., Ushio H., Kohata T., Shioya I., Ohshima T. Lipid oxidations in ordinary and dark muscles of fish: Influences on rancid off-odor development and color darkening of yellowtail flesh during ice storage. Journal of Food Science 2005, 70:490-496.
    • (2005) Journal of Food Science , vol.70 , pp. 490-496
    • Sohn, J.H.1    Taki, Y.2    Ushio, H.3    Kohata, T.4    Shioya, I.5    Ohshima, T.6
  • 32
    • 10944271171 scopus 로고    scopus 로고
    • Krzywicki revisited: Equations for spectrophotometric determination of myoglobin redox forms in aqueous meat extracts
    • Tang J., Faustman C., Hoagland T.A. Krzywicki revisited: Equations for spectrophotometric determination of myoglobin redox forms in aqueous meat extracts. Journal of Food Science 2004, 69:717-720.
    • (2004) Journal of Food Science , vol.69 , pp. 717-720
    • Tang, J.1    Faustman, C.2    Hoagland, T.A.3
  • 33
    • 0032510761 scopus 로고    scopus 로고
    • Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin
    • Tang Q., Kalsbeck W.A., Olson J.S., Bocian D.F. Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin. Biochemistry 1998, 37:7047-7056.
    • (1998) Biochemistry , vol.37 , pp. 7047-7056
    • Tang, Q.1    Kalsbeck, W.A.2    Olson, J.S.3    Bocian, D.F.4
  • 34
    • 0030306591 scopus 로고    scopus 로고
    • A simple, rapid preparative method for isolating and purifying oxymyoglobin
    • Trout G.R., Gutzke D.A. A simple, rapid preparative method for isolating and purifying oxymyoglobin. Meat Science 1996, 43:1-13.
    • (1996) Meat Science , vol.43 , pp. 1-13
    • Trout, G.R.1    Gutzke, D.A.2
  • 35
    • 7544236251 scopus 로고    scopus 로고
    • Primary structure and thermostability of bigeye tuna myoglobin in relation to those of other scombridae fish
    • Ueki N., Ochiai Y. Primary structure and thermostability of bigeye tuna myoglobin in relation to those of other scombridae fish. Fisheries Science 2004, 70:875-884.
    • (2004) Fisheries Science , vol.70 , pp. 875-884
    • Ueki, N.1    Ochiai, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.