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Volumn 127, Issue 2, 2011, Pages 656-661

Equations for spectrophotometric determination of relative concentrations of myoglobin derivatives in aqueous tuna meat extracts

Author keywords

Absorption spectra; Equation; Myoglobin; Spectrophotometric determination; Tuna

Indexed keywords

AQUEOUS EXTRACTS; BLUEFIN TUNA; EQUATION; METMYOGLOBIN; MYOGLOBIN; RELATIVE CONCENTRATION; SPECTROPHOTOMETRIC DETERMINATION; TUNA;

EID: 79952314622     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2011.01.001     Document Type: Article
Times cited : (39)

References (34)
  • 2
    • 34247467012 scopus 로고    scopus 로고
    • Antioxidative activity of carnosine in gamma irradiated ground beef and beef patties
    • Badr, H. M. (2007). Antioxidative activity of carnosine in gamma irradiated ground beef and beef patties. Food Chemistry, 104, 665-679.
    • (2007) Food Chemistry , vol.104 , pp. 665-679
    • Badr, H.M.1
  • 3
    • 0015843337 scopus 로고
    • Equations for the spectrophotometric analysis of hemoglobin mixtures
    • Benesch, R. E., Benesch, R., & Yung, S. (1973). Equations for the spectrophotometric analysis of hemoglobin mixtures. Analytical Biochemistry, 55, 245-248.
    • (1973) Analytical Biochemistry , vol.55 , pp. 245-248
    • Benesch, R.E.1    Benesch, R.2    Yung, S.3
  • 4
    • 0035179693 scopus 로고    scopus 로고
    • Biochemical and physicochemical changes in catfish (Silurus glanis Linne) muscle as influenced by different freeze-thaw cycles
    • DOI 10.1016/S0308-8146(00)00222-3, PII S0308814600002223
    • Benjakul, S., & Bauer, F. (2001). Biochemical and physicochemical changes in catfish (Silurus glani Llinne) muscle as influenced by different freeze-thaw cycles. Food Chemistry, 72, 207-217. (Pubitemid 32013005)
    • (2001) Food Chemistry , vol.72 , Issue.2 , pp. 207-217
    • Benjakul, S.1    Bauer, F.2
  • 5
    • 85007895047 scopus 로고
    • Studies on the retention of meat color of frozen tuna-II. Effect of storage temperature on preventing discoloration of tuna meat during freezing storage
    • Bito, M. (1965). Studies on the retention of meat color of frozen tuna-II. Effect of storage temperature on preventing discoloration of tuna meat during freezing storage. Nippon Suisan Gakkaishi, 31, 534-539.
    • (1965) Nippon Suisan Gakkaishi , vol.31 , pp. 534-539
    • Bito, M.1
  • 7
    • 84958111940 scopus 로고
    • The absorption spectra and extinction coefficients of myoglobin
    • Bowen, B. J. (1949). The absorption spectra and extinction coefficients of myoglobin. Journal Biological Chemistry, 179, 235-245.
    • (1949) Journal Biological Chemistry , vol.179 , pp. 235-245
    • Bowen, B.J.1
  • 8
    • 0011528764 scopus 로고
    • Factors affecting the quality of prepackaged meat. II. E. Determining the proportions of heme derivatives in fresh meat
    • Broumand, H., Ball, C. O., & Stier, E. F. (1958). Factors affecting the quality of prepackaged meat. II. E. Determining the proportions of heme derivatives in fresh meat. Food Technology, 12, 65-77.
    • (1958) Food Technology , vol.12 , pp. 65-77
    • Broumand, H.1    Ball, C.O.2    Stier, E.F.3
  • 11
    • 20444391056 scopus 로고    scopus 로고
    • Changes of pigments and color in sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) muscle during iced storage
    • DOI 10.1016/j.foodchem.2004.10.035, PII S0308814604007812
    • Chaijan, M., Benjakul, S., Visessanguan, W., & Faustman, C. (2005). Changes of pigments and color in sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) muscle during iced storage. Food Chemistry, 93, 607-617. (Pubitemid 40804273)
    • (2005) Food Chemistry , vol.93 , Issue.4 , pp. 607-617
    • Chaijan, M.1    Benjakul, S.2    Visessanguan, W.3    Faustman, C.4
  • 12
    • 33847769501 scopus 로고    scopus 로고
    • Effect of ionic strength and temperature on interaction between fish myoglobin and myofibrillar proteins
    • DOI 10.1111/j.1750-3841.2006.00236.x
    • Chaijan, M., Benjakul, S., Visessanguan, W., Lee, S., & Faustman, C. (2006). Effect of ionic strength and temperature on interaction between fish myoglobin and myofibrillar proteins. Journal of Food Science, 72, C89-C95. (Pubitemid 46392372)
    • (2007) Journal of Food Science , vol.72 , Issue.2
    • Chaijan, M.1    Benjakul, S.2    Visessanguan, W.3    Lee, S.4    Faustman, C.5
  • 13
    • 33745462677 scopus 로고    scopus 로고
    • Characterisation of myoglobin from sardine (Sardinella gibbosa) dark muscle
    • DOI 10.1016/j.foodchem.2005.09.030, PII S0308814605008125
    • Chaijan, M., Benjakul, S., Visessanguan, W., & Faustman, C. (2007). Characterisation of myoglobin from sardine (Sardinella gibbosa) dark muscle. Food Chemistry, 100, 156-164. (Pubitemid 43949316)
    • (2007) Food Chemistry , vol.100 , Issue.1 , pp. 156-164
    • Chaijan, M.1    Benjakul, S.2    Visessanguan, W.3    Faustman, C.4
  • 14
    • 0037851971 scopus 로고    scopus 로고
    • Effect of cold storage on the stability of chub and horse mackerel myoglobins
    • Chen, H.-H. (2003). Effect of cold storage on the stability of chub and horse mackerel myoglobins. Journal of Food Science, 68(4), 1416-1419.
    • (2003) Journal of Food Science , vol.68 , Issue.4 , pp. 1416-1419
    • Chen, H.-H.1
  • 16
    • 84987300648 scopus 로고
    • Color stability, lipid stability, and nutrient composition of red and white veal
    • Faustman, C., Yin, M. C., & Nadeau, D. B. (1992). Color stability, lipid stability, and nutrient composition of red and white veal. Journal of Food Science, 57, 302-304.
    • (1992) Journal of Food Science , vol.57 , pp. 302-304
    • Faustman, C.1    Yin, M.C.2    Nadeau, D.B.3
  • 17
    • 0141675087 scopus 로고    scopus 로고
    • Evaluation of the antioxidant potential of hyssop (Hyssopus officinalis L.) and rosemary (Rosmarinus officinalis L.) extracts in cooked pork meat
    • Fernández-López, J., Sevilla, L., Sayas-Barberá, E., Navarro, C., Marín, F., & Pérez- Alvarez, J. A. (2003). Evaluation of the antioxidant potential of hyssop (Hyssopus officinalis L.) and rosemary (Rosmarinus officinalis L.) extracts in cooked pork meat. Journal of Food Science, 68, 660-664.
    • (2003) Journal of Food Science , vol.68 , pp. 660-664
    • Fernández-López, J.1    Sevilla, L.2    Sayas-Barberá, E.3    Navarro, C.4    Marín, F.5    Pérez-Alvarez, J.A.6
  • 18
    • 0014014360 scopus 로고
    • Turbidity correction for absorption spectra of colored solutions
    • Goldbloom, D. E., & Brown, W. D. (1966). Turbidity correction for absorption spectra of colored solutions. Biochimica et Biophysica Acta, 112, 584-586.
    • (1966) Biochimica et Biophysica Acta , vol.112 , pp. 584-586
    • Goldbloom, D.E.1    Brown, W.D.2
  • 19
    • 85013715938 scopus 로고
    • Factors affecting the rate of metmyoglobin accumulation in prepackaged beef
    • Hood, D. E. (1980). Factors affecting the rate of metmyoglobin accumulation in prepackaged beef. Meat Science, 4, 247-265.
    • (1980) Meat Science , vol.4 , pp. 247-265
    • Hood, D.E.1
  • 20
    • 0003045535 scopus 로고
    • Assessment of relative content of myoglobin, oxymyoglobin and metmyoglobin at the surface of beef
    • Krzywicki, K. (1979). Assessment of relative content of myoglobin, oxymyoglobin and metmyoglobin at the surface of beef. Meat Science, 3, 1-10.
    • (1979) Meat Science , vol.3 , pp. 1-10
    • Krzywicki, K.1
  • 21
    • 0001924192 scopus 로고
    • The determination of haem pigment in meat
    • Krzywicki, K. (1982). The determination of haem pigment in meat. Meat Science, 7, 29-35.
    • (1982) Meat Science , vol.7 , pp. 29-35
    • Krzywicki, K.1
  • 22
    • 0033476636 scopus 로고    scopus 로고
    • A comparison of carnosine and ascorbic acid on color and lipid stability in a ground beef pattie model system
    • Lee, B. J., Hendricks, D. G., & Cornforth, D. P. (1999). A comparison of carnosine and ascorbic acid on color and lipid stability in a ground beef pattie model system. Meat Science, 51, 245-253.
    • (1999) Meat Science , vol.51 , pp. 245-253
    • Lee, B.J.1    Hendricks, D.G.2    Cornforth, D.P.3
  • 23
    • 85007874862 scopus 로고
    • Chemical studies on the red muscle (Chiai) of fishes-IV. Preparation of crystalline myoglobin from the red muscle of fishes
    • in Japanese
    • Matsuura, F., & Hashimoto, K. (1955). Chemical studies on the red muscle (Chiai) of fishes-IV. Preparation of crystalline myoglobin from the red muscle of fishes. Bulletin of the Japanese Society of scientific Fisheries, 20(10), 946-950 (in Japanese).
    • (1955) Bulletin of the Japanese Society of Scientific Fisheries , vol.20 , Issue.10 , pp. 946-950
    • Matsuura, F.1    Hashimoto, K.2
  • 25
    • 79952314146 scopus 로고    scopus 로고
    • Tokyo: Japan Society of Refrigerating and Air Conditioning Engineers in Japanese
    • Takai, R. (2000). Frozen food overview. Frozen food technology. Tokyo: Japan Society of Refrigerating and Air Conditioning Engineers (pp. 1-16). (in Japanese).
    • (2000) Frozen Food Overview. Frozen Food Technology , pp. 1-16
    • Takai, R.1
  • 26
    • 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. (2004). Krzywicki revisited: Equations for spectrophotometric determination of myoglobin redox forms in aqueous meat extracts. Journal of Food Science, 69(9), C717-C720. (Pubitemid 40008809)
    • (2004) Journal of Food Science , vol.69 , Issue.9
    • Tang, J.1    Faustman, C.2    Hoagland, T.A.3
  • 27
    • 0000837366 scopus 로고
    • The rate of metmyoglobin formation in beef, pork, and turkey meat as influenced by pH, sodium chloride, and sodium tripolyphosphate
    • Trout, G. R. (1990). The rate of metmyoglobin formation in beef, pork, and turkey meat as influenced by pH, sodium chloride, and sodium tripolyphosphate. Meat Science, 28, 203-210.
    • (1990) Meat Science , vol.28 , pp. 203-210
    • Trout, G.R.1
  • 28
    • 7544236251 scopus 로고    scopus 로고
    • Primary structure and thermostability of bigeye tuna myoglobin in relation to those of other scombridae fish
    • DOI 10.1111/j.1444-2906.2004.00882.x
    • Ueki, N., & Ochiai, Y. (2004). Primary structure and thermostability of bigeye tuna myoglobin in relation to those of other scombridae fish. Fisheries Science, 70, 875-884. (Pubitemid 39448058)
    • (2004) Fisheries Science , vol.70 , Issue.5 , pp. 875-884
    • Ueki, N.1    Ochiai, Y.2
  • 30
    • 46749100496 scopus 로고    scopus 로고
    • Quantitative measurement of metmyoglobin in tuna flesh via electron paramagnetic resonance
    • Viriyarattanasak, C., Matsukawa, S., Hamada-Sato, N., Watanabe, M., & Suzuki, T. (2008). Quantitative measurement of metmyoglobin in tuna flesh via electron paramagnetic resonance. Food Chemistry, 111, 1050-1056.
    • (2008) Food Chemistry , vol.111 , pp. 1050-1056
    • Viriyarattanasak, C.1    Matsukawa, S.2    Hamada-Sato, N.3    Watanabe, M.4    Suzuki, T.5
  • 31
    • 84991138953 scopus 로고
    • The extraction of haem pigments from fresh meat
    • Warriss, P. D. (1979). The extraction of haem pigments from fresh meat. Journal of Food Technology, 14, 75-80.
    • (1979) Journal of Food Technology , vol.14 , pp. 75-80
    • Warriss, P.D.1
  • 32
    • 0017910680 scopus 로고
    • Analysis of myoglobin derivatives in meat or fish samples using absorption spectrophotometry
    • Wolfe, S. K., Watts, D. A., & Brown, W. D. (1978). Analysis of myoglobin derivatives in meat or fish samples using absorption spectrophotometry. Journal of Agricultural and Food Chemistry, 26, 217-219.
    • (1978) Journal of Agricultural and Food Chemistry , vol.26 , pp. 217-219
    • Wolfe, S.K.1    Watts, D.A.2    Brown, W.D.3
  • 34
    • 0019333181 scopus 로고
    • The primary structure of myoglobin from yellowfin tuna (Thunnus albacares)
    • Watts, D. A., Rice, R. H., & Brown, W. D. (1980). The primary structure of myoglobin from yellowfin tuna (Thunnus albacares). The Journal of Biological Chemistry, 255, 10916-10924.
    • (1980) The Journal of Biological Chemistry , vol.255 , pp. 10916-10924
    • Watts, D.A.1    Rice, R.H.2    Brown, W.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.