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Volumn 17, Issue 1, 2006, Pages 43-55

The effect of epimysial connective tissue on factors related to tenderness of beef semitendinosus

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EID: 33645167499     PISSN: 10460756     EISSN: 17454573     Source Type: Journal    
DOI: 10.1111/j.1745-4573.2006.00033.x     Document Type: Article
Times cited : (6)

References (28)
  • 1
    • 0033244448 scopus 로고    scopus 로고
    • A simple, on-line processing method for improving beef tenderness
    • AALHUS, J.L., BEST, D.R., COSTELLO, F. and JEREMIAH, L.E. 1999. A simple, on-line processing method for improving beef tenderness. Can. J. Anim. Sci. 79, 27-34.
    • (1999) Can. J. Anim. Sci. , vol.79 , pp. 27-34
    • Aalhus, J.L.1    Best, D.R.2    Costello, F.3    Jeremiah, L.E.4
  • 3
    • 84985330464 scopus 로고
    • The basis of meat texture
    • BAILEY, A.J. 1972. The basis of meat texture. J. Sci. Food Agric. 23, 995-1007.
    • (1972) J. Sci. Food Agric. , vol.23 , pp. 995-1007
    • Bailey, A.J.1
  • 5
    • 0037208104 scopus 로고    scopus 로고
    • Warner-Bratzler shear evaluations of 40 bovine muscles
    • BELEW, J.B., BROOKS, J.C., MCKENNA, D.R. and SAVELL, J.W. 2003. Warner-Bratzler shear evaluations of 40 bovine muscles. Meat Sci. 64, 507-512.
    • (2003) Meat Sci. , vol.64 , pp. 507-512
    • Belew, J.B.1    Brooks, J.C.2    McKenna, D.R.3    Savell, J.W.4
  • 6
    • 84982341620 scopus 로고
    • The elastin content of various muscles of beef animals
    • BENDALL, J.R. 1967. The elastin content of various muscles of beef animals. J. Sci. Food Agric. 18, 553-558.
    • (1967) J. Sci. Food Agric. , vol.18 , pp. 553-558
    • Bendall, J.R.1
  • 7
    • 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. and LARSEN, L.M. 2000. The effect of cooking temperature on mechanical properties of whole meat, single muscle fibres and perimysial connective tissue. Meat Sci. 55, 301-307.
    • (2000) Meat Sci. , vol.55 , pp. 301-307
    • Christensen, M.1    Purslow, P.P.2    Larsen, L.M.3
  • 8
    • 0002632645 scopus 로고
    • Assessment of changes in myofibre size in muscle
    • (H. Deboer and J. Martin, eds.), Martinus-Nijhoff, The Hague, the Netherlands
    • CLANCY, M.J. and HERLIHY, P.D. 1978. Assessment of changes in myofibre size in muscle. In Patterns of Growth and Development in Cattle (H. Deboer and J. Martin, eds.) pp. 203-218, Martinus-Nijhoff, The Hague, the Netherlands.
    • (1978) Patterns of Growth and Development in Cattle , pp. 203-218
    • Clancy, M.J.1    Herlihy, P.D.2
  • 9
    • 84987299135 scopus 로고
    • Effects of intra-muscular collagen and elastin on bovine muscle tenderness
    • CROSS, H.R., CARPENTER, Z.L. and SMITH, G.C. 1973. Effects of intra-muscular collagen and elastin on bovine muscle tenderness. J. Food Sci. 38, 998-1003.
    • (1973) J. Food Sci. , vol.38 , pp. 998-1003
    • Cross, H.R.1    Carpenter, Z.L.2    Smith, G.C.3
  • 10
    • 0042357094 scopus 로고    scopus 로고
    • Intramuscular variation in beef tenderness
    • DENOYELLE, C. and LEBIHAN, E. 2003. Intramuscular variation in beef tenderness. Meat Sci. 66, 241-247.
    • (2003) Meat Sci. , vol.66 , pp. 241-247
    • Denoyelle, C.1    Lebihan, E.2
  • 11
    • 0033485257 scopus 로고    scopus 로고
    • Effect of rigor temperature on muscle shortening and tenderisation of restrained and unrestrained beef M. longissimas thoracis et lumborum
    • DEVINE, C.E., WALHGRAN, N.M. and TORNBERG, E. 1999. Effect of rigor temperature on muscle shortening and tenderisation of restrained and unrestrained beef M. longissimas thoracis et lumborum. Meat Sci. 51, 61-72.
    • (1999) Meat Sci. , vol.51 , pp. 61-72
    • Devine, C.E.1    Walhgran, N.M.2    Tornberg, E.3
  • 12
    • 27144472239 scopus 로고    scopus 로고
    • A mapping method for the description of Warner-Bratzler shear force gradients in beef Longissimus thoracis et lumborum and Semitendinosus
    • JANZ, J.A.M., AALHUS, J.L., DUGAN, M.E.R. and PRICE, M.A. 2006. A mapping method for the description of Warner-Bratzler shear force gradients in beef Longissimus thoracis et lumborum and Semitendinosus. Meat Sci. 72, 79-90.
    • (2006) Meat Sci. , vol.72 , pp. 79-90
    • Janz, J.A.M.1    Aalhus, J.L.2    Dugan, M.E.R.3    Price, M.A.4
  • 13
    • 0033373057 scopus 로고    scopus 로고
    • The influence of mechanical tenderization on the palatability of certain bovine muscles
    • JEREMIAH, L.E., GIBSON, L.L. and CUNNINGHAM, G. 1999. The influence of mechanical tenderization on the palatability of certain bovine muscles. Food Res. Int. 32, 585-591.
    • (1999) Food Res. Int. , vol.32 , pp. 585-591
    • Jeremiah, L.E.1    Gibson, L.L.2    Cunningham, G.3
  • 14
  • 15
    • 23044496428 scopus 로고
    • Relationship of collagen content, type and cross-linking with texture of different muscles
    • LIGHT, N.D., RESTALL, D.J. and BAILEY, A.J. 1984. Relationship of collagen content, type and cross-linking with texture of different muscles. Proc. Eur. Meat Res. Workers Mtg. 30, 139-140.
    • (1984) Proc. Eur. Meat Res. Workers Mtg. , vol.30 , pp. 139-140
    • Light, N.D.1    Restall, D.J.2    Bailey, A.J.3
  • 18
    • 0001253294 scopus 로고
    • Comparison of the amino acid composition and connective tissue protein contents of selected bovine skeletal muscles
    • NGUYEN, Q. and ZARKADAS, C.G. 1989. Comparison of the amino acid composition and connective tissue protein contents of selected bovine skeletal muscles. J. Agr. Food Chem. 37, 1279-1286.
    • (1989) J. Agr. Food Chem. , vol.37 , pp. 1279-1286
    • Nguyen, Q.1    Zarkadas, C.G.2
  • 19
    • 0033481199 scopus 로고    scopus 로고
    • Changes in texture, cooking losses, and myofibrillar structure of bovine M. semitendinosus during heating
    • PALKA, K. and DAUN, H. 1999. Changes in texture, cooking losses, and myofibrillar structure of bovine M. semitendinosus during heating. Meat Sci. 57, 237-243.
    • (1999) Meat Sci. , vol.57 , pp. 237-243
    • Palka, K.1    Daun, H.2
  • 20
    • 0031267271 scopus 로고    scopus 로고
    • Carcass characteristics, the calpain proteinase system, and aged tenderness of Angus and Brahman crossbred steers
    • PRINGLE, T.D., WILLIAMS, S.E., LAMB, B.S., JOHNSON, D.D. and WEST, R.L. 1997. Carcass characteristics, the calpain proteinase system, and aged tenderness of Angus and Brahman crossbred steers. J. Anim. Sci. 75, 2955-2961.
    • (1997) J. Anim. Sci. , vol.75 , pp. 2955-2961
    • Pringle, T.D.1    Williams, S.E.2    Lamb, B.S.3    Johnson, D.D.4    West, R.L.5
  • 21
    • 0036782839 scopus 로고    scopus 로고
    • Mapping intramuscular tenderness variation in four major muscles of the beef round
    • REUTER, B.J., WULF, D.M. and MADDOCK, R.J. 2002. Mapping intramuscular tenderness variation in four major muscles of the beef round. J. Anim. Sci. 80, 2594-2599.
    • (2002) J. Anim. Sci. , vol.80 , pp. 2594-2599
    • Reuter, B.J.1    Wulf, D.M.2    Maddock, R.J.3
  • 23
    • 0040585204 scopus 로고
    • Identification of threshold levels for Warner-Bratzler shear force in beef top loin steaks
    • SHACKELFORD, S.D., MORGAN, J.B., CROSS, H.R. and SAVELL, J.W. 1991. Identification of threshold levels for Warner-Bratzler shear force in beef top loin steaks. J. Muscle Foods 2, 289-296.
    • (1991) J. Muscle Foods , vol.2 , pp. 289-296
    • Shackelford, S.D.1    Morgan, J.B.2    Cross, H.R.3    Savell, J.W.4
  • 24
    • 0031228305 scopus 로고    scopus 로고
    • Repeatability of tenderness measurements in beef round muscles
    • SHACKELFORD, S.D., WHEELER, T.L. and KOOHMARAIE, M. 1997. Repeatability of tenderness measurements in beef round muscles. J. Anim. Sci. 75, 2411-2416.
    • (1997) J. Anim. Sci. , vol.75 , pp. 2411-2416
    • Shackelford, S.D.1    Wheeler, T.L.2    Koohmaraie, M.3
  • 25
    • 0001839832 scopus 로고
    • The effects of conditioning on meat collagen. Part 3: Evidence for proteolytic damage to endomysial collagen after conditioning
    • STANTON, C. and LIGHT, N. 1990. The effects of conditioning on meat collagen. Part 3: Evidence for proteolytic damage to endomysial collagen after conditioning. Meat Sci. 27, 41-54.
    • (1990) Meat Sci. , vol.27 , pp. 41-54
    • Stanton, C.1    Light, N.2
  • 26
    • 43949172570 scopus 로고
    • Structural studies of rigor bovine myofibrils using fluorescence microcopy. II: Influence of sarcomere length on the binding of myosin subfragment-1, alpha-actinin and G-actin to rigor myofibrils
    • SWARTZ, D.R., GREASER, M.L. and MARSH, B.B. 1993. Structural studies of rigor bovine myofibrils using fluorescence microcopy. II: Influence of sarcomere length on the binding of myosin subfragment-1, alpha-actinin and G-actin to rigor myofibrils. Meat Sci. 33, 157-190.
    • (1993) Meat Sci. , vol.33 , pp. 157-190
    • Swartz, D.R.1    Greaser, M.L.2    Marsh, B.B.3
  • 28
    • 0034101635 scopus 로고    scopus 로고
    • Pre-rigor conditions in beef under varying temperature- and pH-falls studied with rigometer, NMR and NIR
    • TORNBERG, E., WALHGREN, M., BRØNDUM, J. and ENGELSEN, S.B. 2000. Pre-rigor conditions in beef under varying temperature- and pH-falls studied with rigometer, NMR and NIR. Food Chem. 69, 407-418.
    • (2000) Food Chem. , vol.69 , pp. 407-418
    • Tornberg, E.1    Walhgren, M.2    Brøndum, J.3    Engelsen, S.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.