메뉴 건너뛰기




Volumn 123, Issue 2, 2010, Pages 456-464

Near-infrared oximetry of three post-rigor skeletal muscles for following myoglobin redox forms

Author keywords

Meat colour; Modified atmosphere packaging; Myoglobin redox forms; Near infrared tissue oximeter; Reflectance spectroscopy

Indexed keywords

DEOXYMYOGLOBIN; METMYOGLOBIN; MYOGLOBIN; OXYMYOGLOBIN; UNCLASSIFIED DRUG;

EID: 77953287292     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2010.04.068     Document Type: Article
Times cited : (16)

References (28)
  • 2
    • 0015355325 scopus 로고
    • Consumption of oxygen by the muscles of beef animals and related species. II. Consumption of oxygen by post-rigor muscle
    • Bendall J.R., and Taylor A.A. Consumption of oxygen by the muscles of beef animals and related species. II. Consumption of oxygen by post-rigor muscle. Journal of the Science of Food and Agriculture 23 6 (1972) 707-719
    • (1972) Journal of the Science of Food and Agriculture , vol.23 , Issue.6 , pp. 707-719
    • Bendall, J.R.1    Taylor, A.A.2
  • 3
    • 84958111940 scopus 로고
    • The absorption spectra and extinction coefficients of myoglobin
    • Bowen W.J. The absorption spectra and extinction coefficients of myoglobin. The Journal of Biological Chemistry 179 1 (1949) 235-245
    • (1949) The Journal of Biological Chemistry , vol.179 , Issue.1 , pp. 235-245
    • Bowen, W.J.1
  • 6
    • 84987260388 scopus 로고
    • A Study of the rate-limiting factors in the respiratory oxygen consumption of intact post-rigor bovine muscle
    • DeVore D.P., and Solberg M. A Study of the rate-limiting factors in the respiratory oxygen consumption of intact post-rigor bovine muscle. Journal of Food Science 40 3 (1975) 651-652
    • (1975) Journal of Food Science , vol.40 , Issue.3 , pp. 651-652
    • DeVore, D.P.1    Solberg, M.2
  • 8
    • 0035132870 scopus 로고    scopus 로고
    • Non-invasive and quantitative near-infrared haemoglobin spectrometry in the piglet brain during hypoxic stress, using a frequency-domain multidistance instrument
    • Hueber D., Franceschini M., Ma H., Zhang Q., Ballesteros J., Fantini S., et al. Non-invasive and quantitative near-infrared haemoglobin spectrometry in the piglet brain during hypoxic stress, using a frequency-domain multidistance instrument. Physics in Medicine and Biology 46 1 (2001) 41-62
    • (2001) Physics in Medicine and Biology , vol.46 , Issue.1 , pp. 41-62
    • Hueber, D.1    Franceschini, M.2    Ma, H.3    Zhang, Q.4    Ballesteros, J.5    Fantini, S.6
  • 10
    • 84987280052 scopus 로고
    • Profile of fiber types and related properties of five bovine muscles
    • Hunt M., and Hedrick H. Profile of fiber types and related properties of five bovine muscles. Journal of Food Science 42 2 (1977) 513-517
    • (1977) Journal of Food Science , vol.42 , Issue.2 , pp. 513-517
    • Hunt, M.1    Hedrick, H.2
  • 11
    • 84987317170 scopus 로고
    • Histochemical and histological characteristics of bovine muscles from four quality groups
    • Hunt M., and Hedrick H. Histochemical and histological characteristics of bovine muscles from four quality groups. Journal of Food Science 42 3 (1977) 578-582
    • (1977) Journal of Food Science , vol.42 , Issue.3 , pp. 578-582
    • Hunt, M.1    Hedrick, H.2
  • 12
    • 1342266100 scopus 로고    scopus 로고
    • Rapid determination of moisture and fat in meats by microwave and nuclear magnetic resonance analysis - PVM 1:2003
    • Keeton J.T., Hafley B.S., Eddy S.M., Moser C.R., McManus B.J., and Leffler T.P. Rapid determination of moisture and fat in meats by microwave and nuclear magnetic resonance analysis - PVM 1:2003. Journal of AOAC International 86 6 (2003) 1193-1202
    • (2003) Journal of AOAC International , vol.86 , Issue.6 , pp. 1193-1202
    • Keeton, J.T.1    Hafley, B.S.2    Eddy, S.M.3    Moser, C.R.4    McManus, B.J.5    Leffler, T.P.6
  • 13
    • 0001348724 scopus 로고
    • Colour stability: factors affecting the colour of fresh meat
    • Kropf D. Colour stability: factors affecting the colour of fresh meat. Meat Focus International 2 6 (1993) 269-275
    • (1993) Meat Focus International , vol.2 , Issue.6 , pp. 269-275
    • Kropf, D.1
  • 14
    • 10544229564 scopus 로고
    • Mitochondrial activity and beef muscle colour stability
    • Lanari M., and Cassens R. Mitochondrial activity and beef muscle colour stability. Journal of Food Science 56 6 (1991) 1476-1479
    • (1991) Journal of Food Science , vol.56 , Issue.6 , pp. 1476-1479
    • Lanari, M.1    Cassens, R.2
  • 15
    • 0001306887 scopus 로고
    • Aging and processing affect colour, metmyoglobin reductase and oxygen consumption of beef muscles
    • Madhavi D., and Carpenter C.E. Aging and processing affect colour, metmyoglobin reductase and oxygen consumption of beef muscles. Journal of Food Science 58 5 (1993) 939-942
    • (1993) Journal of Food Science , vol.58 , Issue.5 , pp. 939-942
    • Madhavi, D.1    Carpenter, C.E.2
  • 16
    • 22144493345 scopus 로고    scopus 로고
    • Current research in meat colour
    • Mancini R., and Hunt M. Current research in meat colour. Meat Science 71 1 (2005) 100-121
    • (2005) Meat Science , vol.71 , Issue.1 , pp. 100-121
    • Mancini, R.1    Hunt, M.2
  • 17
    • 0037208120 scopus 로고    scopus 로고
    • Reflectance at 610 nanometers estimates oxymyoglobin content on the surface of ground beef
    • Mancini R., Hunt M., and Kropf D. Reflectance at 610 nanometers estimates oxymyoglobin content on the surface of ground beef. Meat Science 64 2 (2003) 157-162
    • (2003) Meat Science , vol.64 , Issue.2 , pp. 157-162
    • Mancini, R.1    Hunt, M.2    Kropf, D.3
  • 18
    • 34250714943 scopus 로고    scopus 로고
    • Wavelength shift analysis: a simple method to determine the contribution of hemoglobin and myoglobin to in vivo optical spectra
    • Marcinek D.J., Amara C.E., Matz K., Conley K.E., and Schenkman K.A. Wavelength shift analysis: a simple method to determine the contribution of hemoglobin and myoglobin to in vivo optical spectra. Applied Spectroscopy 61 6 (2007) 665-669
    • (2007) Applied Spectroscopy , vol.61 , Issue.6 , pp. 665-669
    • Marcinek, D.J.1    Amara, C.E.2    Matz, K.3    Conley, K.E.4    Schenkman, K.A.5
  • 19
    • 18844374883 scopus 로고    scopus 로고
    • Biochemical and physical factors affecting discolouration characteristics of 19 bovine muscles
    • McKenna D., Mies P., Baird B., Pfeiffer K., Ellebracht J., and Savell J. Biochemical and physical factors affecting discolouration characteristics of 19 bovine muscles. Meat Science 70 4 (2005) 665-682
    • (2005) Meat Science , vol.70 , Issue.4 , pp. 665-682
    • McKenna, D.1    Mies, P.2    Baird, B.3    Pfeiffer, K.4    Ellebracht, J.5    Savell, J.6
  • 20
    • 0000544177 scopus 로고
    • Muscle hemoglobin
    • Millikan G. Muscle hemoglobin. Physiological Reviews 19 4 (1939) 503-523
    • (1939) Physiological Reviews , vol.19 , Issue.4 , pp. 503-523
    • Millikan, G.1
  • 21
    • 70349751949 scopus 로고    scopus 로고
    • Effects of fiber orientation, myoglobin redox form, and postmortem storage on NIR tissue oximeter measurements of beef Longissimus muscle
    • Mohan A., Hunt M.C., Barstow T.J., Houser T.A., Bopp C., and Hueber D.M. Effects of fiber orientation, myoglobin redox form, and postmortem storage on NIR tissue oximeter measurements of beef Longissimus muscle. Meat Science 84 1 (2009) 79-85
    • (2009) Meat Science , vol.84 , Issue.1 , pp. 79-85
    • Mohan, A.1    Hunt, M.C.2    Barstow, T.J.3    Houser, T.A.4    Bopp, C.5    Hueber, D.M.6
  • 22
    • 0000670411 scopus 로고
    • Biochemical factors influencing metmyoglobin formation on beef from muscles of differing colour stability
    • O'Keefe M., and Hood D. Biochemical factors influencing metmyoglobin formation on beef from muscles of differing colour stability. Meat Science 7 3 (1982) 209-228
    • (1982) Meat Science , vol.7 , Issue.3 , pp. 209-228
    • O'Keefe, M.1    Hood, D.2
  • 23
    • 0001362225 scopus 로고
    • Biochemical factors influencing metmyoglobin formation in beef muscles
    • Renerre M., and Labas R. Biochemical factors influencing metmyoglobin formation in beef muscles. Meat Science 19 2 (1987) 151-165
    • (1987) Meat Science , vol.19 , Issue.2 , pp. 151-165
    • Renerre, M.1    Labas, R.2
  • 24
    • 0036265726 scopus 로고    scopus 로고
    • Comparison of assays for metmyoglobin reducing ability in beef inside and outside semimembranosus muscle
    • Sammel L., Hunt M., Kropf D., Hachmeister K., and Johnson D. Comparison of assays for metmyoglobin reducing ability in beef inside and outside semimembranosus muscle. Journal of Food Science 67 3 (2002) 978-984
    • (2002) Journal of Food Science , vol.67 , Issue.3 , pp. 978-984
    • Sammel, L.1    Hunt, M.2    Kropf, D.3    Hachmeister, K.4    Johnson, D.5
  • 27
    • 63649132124 scopus 로고    scopus 로고
    • Evaluation of analytical methods for the determination of moisture, crude protein, crude fat, and crude fiber in distillers dried grains with solubles
    • Thiex N. Evaluation of analytical methods for the determination of moisture, crude protein, crude fat, and crude fiber in distillers dried grains with solubles. Journal of AOAC International 92 1 (2009) 61-73
    • (2009) Journal of AOAC International , vol.92 , Issue.1 , pp. 61-73
    • Thiex, N.1
  • 28
    • 84982066590 scopus 로고
    • The post-mortem oxygen requirements of bovine tissue a
    • Urbin M., and Wilson G. The post-mortem oxygen requirements of bovine tissue a. Journal of Food Science 26 3 (1961) 314-317
    • (1961) Journal of Food Science , vol.26 , Issue.3 , pp. 314-317
    • Urbin, M.1    Wilson, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.