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Volumn 93, Issue 4, 2013, Pages 787-795

Relationship between meat toughness and properties of connective tissue from cows and young bulls heat treated at low temperatures for prolonged times

Author keywords

Beef; Cathepsin; Collagen; Denaturation; Hyper spectral imaging; Sous vide

Indexed keywords

CATHEPSIN; COMBINED EFFECT; CONFORMATIONAL CHANGE; CONNECTIVE TISSUES; HEATING TEMPERATURES; HEATING TIME; HYPERSPECTRAL IMAGING; LOW TEMPERATURES; PROTEIN DENATURATION; SEMITENDINOSUS MUSCLES; SOUS-VIDE;

EID: 84872178148     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2012.12.001     Document Type: Article
Times cited : (104)

References (40)
  • 1
    • 0004604644 scopus 로고
    • Proteases cathepsins - A view
    • Agarwal S.K. Proteases cathepsins - A view. Biochemical Education 1990, 18(2):67-72.
    • (1990) Biochemical Education , vol.18 , Issue.2 , pp. 67-72
    • Agarwal, S.K.1
  • 3
    • 9644291525 scopus 로고    scopus 로고
    • Cleavage of desmin by cysteine proteases: Calpains and cathepsin B
    • Baron C.P., Jacobsen S., Purslow P.P. Cleavage of desmin by cysteine proteases: Calpains and cathepsin B. Meat Science 2004, 68(3):447-456.
    • (2004) Meat Science , vol.68 , Issue.3 , pp. 447-456
    • Baron, C.P.1    Jacobsen, S.2    Purslow, P.P.3
  • 4
    • 0000447069 scopus 로고
    • Some effects on the mechanical-properties of meat produced by cooking at temperatures between 50-degrees and 60-degrees-C
    • Beilken S.L., Bouton P.E., Harris P.V. Some effects on the mechanical-properties of meat produced by cooking at temperatures between 50-degrees and 60-degrees-C. Journal of Food Science 1986, 51(3):791-796.
    • (1986) Journal of Food Science , vol.51 , Issue.3 , pp. 791-796
    • Beilken, S.L.1    Bouton, P.E.2    Harris, P.V.3
  • 5
    • 0011658974 scopus 로고
    • Comparative action of cathepsin-B and cathepsin-L on intramuscular collagen as assessed by differential scanning calorimetry
    • Beltran J., Bonnet M., Ouali A. Comparative action of cathepsin-B and cathepsin-L on intramuscular collagen as assessed by differential scanning calorimetry. Meat Science 1992, 32(3):299-306.
    • (1992) Meat Science , vol.32 , Issue.3 , pp. 299-306
    • Beltran, J.1    Bonnet, M.2    Ouali, A.3
  • 6
    • 84982341620 scopus 로고
    • The elastin content of various muscles of beef animals
    • Bendall J.R. The elastin content of various muscles of beef animals. Journal of the Science of Food and Agriculture 1967, 18(12):553-558.
    • (1967) Journal of the Science of Food and Agriculture , vol.18 , Issue.12 , pp. 553-558
    • Bendall, J.R.1
  • 7
  • 8
    • 84987265375 scopus 로고
    • Effects of cooking temperature and time on some mechanical properties of meat
    • Bouton P.E., Harris P.V. Effects of cooking temperature and time on some mechanical properties of meat. Journal of Food Science 1972, 37(1):140-144.
    • (1972) Journal of Food Science , vol.37 , Issue.1 , pp. 140-144
    • Bouton, P.E.1    Harris, P.V.2
  • 9
    • 84985275101 scopus 로고
    • Changes in the tenderness of meat cooked at 50-65-degrees-C
    • Bouton P.E., Harris P.V. Changes in the tenderness of meat cooked at 50-65-degrees-C. Journal of Food Science 1981, 46(2):475-478.
    • (1981) Journal of Food Science , vol.46 , Issue.2 , pp. 475-478
    • Bouton, P.E.1    Harris, P.V.2
  • 10
    • 0001657132 scopus 로고
    • Changes in shear parameters of meat associated with structural-changes produced by aging, cooking and myofibrillar contraction
    • Bouton P.E., Harris P.V., Shorthose W.R. Changes in shear parameters of meat associated with structural-changes produced by aging, cooking and myofibrillar contraction. Journal of Food Science 1975, 40(6):1122-1126.
    • (1975) Journal of Food Science , vol.40 , Issue.6 , pp. 1122-1126
    • Bouton, P.E.1    Harris, P.V.2    Shorthose, W.R.3
  • 11
    • 0037826648 scopus 로고
    • Qualities of beef as affected by cooking at very low temperatures for long periods of time
    • Bramblett V.D., Hostetler R.L., Vail G.E., Draudt H.N. Qualities of beef as affected by cooking at very low temperatures for long periods of time. Food Technology 1959, 13(12):707-711.
    • (1959) Food Technology , vol.13 , Issue.12 , pp. 707-711
    • Bramblett, V.D.1    Hostetler, R.L.2    Vail, G.E.3    Draudt, H.N.4
  • 12
    • 77955090953 scopus 로고
    • Further studies on qualities of beef as affected by cooking at very low temperatures for long periods
    • Bramblett V.D., Vail G.E. Further studies on qualities of beef as affected by cooking at very low temperatures for long periods. Food Technology 1964, 18(2):245-247.
    • (1964) Food Technology , vol.18 , Issue.2 , pp. 245-247
    • Bramblett, V.D.1    Vail, G.E.2
  • 13
    • 76549132629 scopus 로고    scopus 로고
    • Second harmonic generation microscopy: a tool for spatially and temporally resolved studies of heat induced structural changes in meat
    • Brüggemann D.A., Brewer J., Risbo J., Bagatolli L. Second harmonic generation microscopy: a tool for spatially and temporally resolved studies of heat induced structural changes in meat. Food Biophysics 2010, 5(1):1-8.
    • (2010) Food Biophysics , vol.5 , Issue.1 , pp. 1-8
    • Brüggemann, D.A.1    Brewer, J.2    Risbo, J.3    Bagatolli, L.4
  • 14
    • 0015984017 scopus 로고
    • Cathepsin-B1 - lysosomal enzyme that degrades native collagen
    • Burleigh M.C., Barrett A.J., Lazarus G.S. Cathepsin-B1 - lysosomal enzyme that degrades native collagen. Biochemical Journal 1974, 137(2):387-398.
    • (1974) Biochemical Journal , vol.137 , Issue.2 , pp. 387-398
    • Burleigh, M.C.1    Barrett, A.J.2    Lazarus, G.S.3
  • 15
    • 79955049228 scopus 로고    scopus 로고
    • Protein denaturation and water-protein interactions as affected by low temperature long time treatment of porcine longissimus dorsi
    • Christensen L., Bertram H.C., Aaslyng M.D., Christensen M. Protein denaturation and water-protein interactions as affected by low temperature long time treatment of porcine longissimus dorsi. Meat Science 2011, 88(4):718-722.
    • (2011) Meat Science , vol.88 , Issue.4 , pp. 718-722
    • Christensen, L.1    Bertram, H.C.2    Aaslyng, M.D.3    Christensen, M.4
  • 16
    • 79951770929 scopus 로고    scopus 로고
    • Effect of prolonged heat treatment from 48C to 63C on toughness, cooking loss and color of pork
    • Christensen L., Ertbjerg P., Aaslyng M.D., Christensen M. Effect of prolonged heat treatment from 48C to 63C on toughness, cooking loss and color of pork. Meat Science 2011, 88(2):280-285.
    • (2011) Meat Science , vol.88 , Issue.2 , pp. 280-285
    • Christensen, L.1    Ertbjerg, P.2    Aaslyng, M.D.3    Christensen, M.4
  • 18
    • 0034375314 scopus 로고    scopus 로고
    • The effect of cooking temperature on mechanical properties of whole meat, single muscle fibres and perimysial connective tissue
    • Christensen M., Purslow P.P., Larsen L.M. The effect of cooking temperature on mechanical properties of whole meat, single muscle fibres and perimysial connective tissue. Meat Science 2000, 55(3):301-307.
    • (2000) Meat Science , vol.55 , Issue.3 , pp. 301-307
    • Christensen, M.1    Purslow, P.P.2    Larsen, L.M.3
  • 19
    • 84355161380 scopus 로고    scopus 로고
    • Physico-chemical, textural and structural characteristics of sous-vide cooked pork cheeks as affected by vacuum, cooking temperature, and cooking time
    • del Pulgar J.S., Gazquez A., Ruiz-Carrascal J. Physico-chemical, textural and structural characteristics of sous-vide cooked pork cheeks as affected by vacuum, cooking temperature, and cooking time. Meat Science 2012, 90(3):828-835.
    • (2012) Meat Science , vol.90 , Issue.3 , pp. 828-835
    • del Pulgar, J.S.1    Gazquez, A.2    Ruiz-Carrascal, J.3
  • 23
    • 0032748736 scopus 로고    scopus 로고
    • Color and heat denaturation of myoglobin forms in ground Beef
    • Hunt M.C., Sørheim O., Slinde E. Color and heat denaturation of myoglobin forms in ground Beef. Journal of Food Science 1999, 64(5):847-851.
    • (1999) Journal of Food Science , vol.64 , Issue.5 , pp. 847-851
    • Hunt, M.C.1    Sørheim, O.2    Slinde, E.3
  • 24
    • 0025078028 scopus 로고
    • Colorimetric determination of hydroxyproline as measure of collagen content in meat and meat-products - NMKL collaborative study
    • Kolar K. Colorimetric determination of hydroxyproline as measure of collagen content in meat and meat-products - NMKL collaborative study. Journal of the Association of Official Analytical Chemists 1990, 73(1):54-57.
    • (1990) Journal of the Association of Official Analytical Chemists , vol.73 , Issue.1 , pp. 54-57
    • Kolar, K.1
  • 25
    • 0026591107 scopus 로고
    • The role of Ca-2+-dependent proteases (calpains) in postmortem proteolysis and meat tenderness
    • Koohmaraie M. The role of Ca-2+-dependent proteases (calpains) in postmortem proteolysis and meat tenderness. Biochimie 1992, 74(3):239-245.
    • (1992) Biochimie , vol.74 , Issue.3 , pp. 239-245
    • Koohmaraie, M.1
  • 26
    • 84986500333 scopus 로고
    • Low-temperature, long-time heating of bovine muscle. 3. Collagenolytic activity
    • Laakkonen E., Sherbon J.W., Wellington G.H. Low-temperature, long-time heating of bovine muscle. 3. Collagenolytic activity. Journal of Food Science 1970, 35(2):181-183.
    • (1970) Journal of Food Science , vol.35 , Issue.2 , pp. 181-183
    • Laakkonen, E.1    Sherbon, J.W.2    Wellington, G.H.3
  • 27
    • 84986518888 scopus 로고
    • Low-temperature, long-time heating of bovine muscle 1. changes in tenderness, water-binding capacity, pH and amount of water-soluble components
    • Laakkonen E., Wellington G.H., Sherbon J.W. Low-temperature, long-time heating of bovine muscle 1. changes in tenderness, water-binding capacity, pH and amount of water-soluble components. Journal of Food Science 1970, 35(2):175-177.
    • (1970) Journal of Food Science , vol.35 , Issue.2 , pp. 175-177
    • Laakkonen, E.1    Wellington, G.H.2    Sherbon, J.W.3
  • 28
    • 33847145736 scopus 로고    scopus 로고
    • A theoretical approach of the relationships between collagen content, collagen cross-links and meat tenderness
    • Lepetit J. A theoretical approach of the relationships between collagen content, collagen cross-links and meat tenderness. Meat Science 2007, 76(1):147-159.
    • (2007) Meat Science , vol.76 , Issue.1 , pp. 147-159
    • Lepetit, J.1
  • 29
    • 0042350970 scopus 로고    scopus 로고
    • Modelling the effect of sarcomere length on collagen thermal shortening in cooked meat: consequence on meat toughness
    • Lepetit J., Grajales A., Favier R. Modelling the effect of sarcomere length on collagen thermal shortening in cooked meat: consequence on meat toughness. Meat Science 2000, 54(3):239-250.
    • (2000) Meat Science , vol.54 , Issue.3 , pp. 239-250
    • Lepetit, J.1    Grajales, A.2    Favier, R.3
  • 30
    • 84981870744 scopus 로고
    • Effect of heating time and temperature on shear of beef semitendinosus muscle
    • Machlik S.M., Draudt H.N. Effect of heating time and temperature on shear of beef semitendinosus muscle. Journal of Food Science 1963, 28(6):711-718.
    • (1963) Journal of Food Science , vol.28 , Issue.6 , pp. 711-718
    • Machlik, S.M.1    Draudt, H.N.2
  • 31
    • 0032056272 scopus 로고    scopus 로고
    • The effects of age at slaughter, genotype and finishing system on the biochemical properties, muscle fibre type characteristics and eating quality of bull beef from suckled calves
    • Maltin C.A., Sinclair K.D., Warriss P.D., Grant C.M., Porter A.D., Delday M.I., Warkup C.C. The effects of age at slaughter, genotype and finishing system on the biochemical properties, muscle fibre type characteristics and eating quality of bull beef from suckled calves. Animal Science 1998, 66(02):341.
    • (1998) Animal Science , vol.66 , Issue.2 , pp. 341
    • Maltin, C.A.1    Sinclair, K.D.2    Warriss, P.D.3    Grant, C.M.4    Porter, A.D.5    Delday, M.I.6    Warkup, C.C.7
  • 32
    • 84981378480 scopus 로고
    • Texture and color changes in meat during cooking related to thermal-denaturation of muscle proteins
    • Martens H., Stabursvik E., Martens M. Texture and color changes in meat during cooking related to thermal-denaturation of muscle proteins. Journal of Texture Studies 1982, 13(3):291-309.
    • (1982) Journal of Texture Studies , vol.13 , Issue.3 , pp. 291-309
    • Martens, H.1    Stabursvik, E.2    Martens, M.3
  • 33
    • 0000505192 scopus 로고
    • Analysis of Warner-Bratzler shear pattern with regard to myofibrillar and connective-tissue components of tenderness
    • Møller A.J. Analysis of Warner-Bratzler shear pattern with regard to myofibrillar and connective-tissue components of tenderness. Meat Science 1981, 5(4):247-260.
    • (1981) Meat Science , vol.5 , Issue.4 , pp. 247-260
    • Møller, A.J.1
  • 34
    • 84858632385 scopus 로고    scopus 로고
    • Effect of time and temperature on sensory properties in low-temperature long-time sous-vide cooking of beef
    • Mortensen L.M., Frøst M.B., Skibsted L.H., Risbo J. Effect of time and temperature on sensory properties in low-temperature long-time sous-vide cooking of beef. Journal of Culinary Science and Technology 2012, 10:75-109.
    • (2012) Journal of Culinary Science and Technology , vol.10 , pp. 75-109
    • Mortensen, L.M.1    Frøst, M.B.2    Skibsted, L.H.3    Risbo, J.4
  • 35
    • 33645179299 scopus 로고
    • Assessment of the previous heat-treatment given to meat-products in the temperature-range 40-degrees-C-90-degrees-C. 2. Differential scanning calorimetry, a preliminary-study
    • Parsons S., Pattersons R. Assessment of the previous heat-treatment given to meat-products in the temperature-range 40-degrees-C-90-degrees-C. 2. Differential scanning calorimetry, a preliminary-study. Journal of Food Technology 1986, 21(2):123-131.
    • (1986) Journal of Food Technology , vol.21 , Issue.2 , pp. 123-131
    • Parsons, S.1    Pattersons, R.2
  • 36
    • 38249042300 scopus 로고
    • Elastin in bovine semitendinosus and longissimus dorsi muscles
    • Rowe R.W.D. Elastin in bovine semitendinosus and longissimus dorsi muscles. Meat Science 1986, 17(4):293-312.
    • (1986) Meat Science , vol.17 , Issue.4 , pp. 293-312
    • Rowe, R.W.D.1
  • 37
    • 0000597728 scopus 로고
    • Meat tenderness: Age related changes in bovine intramuscular collagen
    • Shimokomaki M., Elsden D.F., Bailey A.J. Meat tenderness: Age related changes in bovine intramuscular collagen. Journal of Food Science 1972, 37(6):892-896.
    • (1972) Journal of Food Science , vol.37 , Issue.6 , pp. 892-896
    • Shimokomaki, M.1    Elsden, D.F.2    Bailey, A.J.3
  • 38
    • 84985298551 scopus 로고
    • Thermal-denaturation of proteins in post-rigor muscle-tissue as studied by differential scanning calorimetry
    • Stabursvik E., Martens H. Thermal-denaturation of proteins in post-rigor muscle-tissue as studied by differential scanning calorimetry. Journal of the Science of Food and Agriculture 1980, 31(10):1034-1042.
    • (1980) Journal of the Science of Food and Agriculture , vol.31 , Issue.10 , pp. 1034-1042
    • Stabursvik, E.1    Martens, H.2
  • 39
    • 33644522736 scopus 로고    scopus 로고
    • Effects of heat on meat proteins-Implications on structure and quality of meat products
    • Tornberg E. Effects of heat on meat proteins-Implications on structure and quality of meat products. Meat Science 2005, 70(3):493-508.
    • (2005) Meat Science , vol.70 , Issue.3 , pp. 493-508
    • Tornberg, E.1
  • 40
    • 52249083447 scopus 로고    scopus 로고
    • Comparison of the thermal characteristics of connective tissue in loose structured and normal structured porcine M. semimembranosus
    • Voutila L., Ruusunen M., Puolanne E. Comparison of the thermal characteristics of connective tissue in loose structured and normal structured porcine M. semimembranosus. Meat Science 2008, 80(4):1024-1030.
    • (2008) Meat Science , vol.80 , Issue.4 , pp. 1024-1030
    • Voutila, L.1    Ruusunen, M.2    Puolanne, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.