메뉴 건너뛰기




Volumn 61, Issue 2, 2002, Pages 205-214

Tenderness of pork m. longissimus thoracis et lumborum after accelerated boning. Part I. Effect of temperature conditioning

Author keywords

Ageing; Cold toughening; Pork hot boning; Temperature conditioning

Indexed keywords

COLD TOUGHENING;

EID: 0036309401     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0309-1740(01)00188-7     Document Type: Article
Times cited : (21)

References (44)
  • 1
    • 0037598922 scopus 로고
    • Use of electrical stimulation for hot boning of meat
    • A. M. Pearson, & T. R. Dutson (Eds.) Connecticut: AVI Publishing Co Inc.
    • Cross, H. R., & Seideman, S. C. (1985). Use of electrical stimulation for hot boning of meat. In A. M. Pearson, & T. R. Dutson (Eds.), Advances in meat research. Electrical stimulation Vol. 1. Connecticut: AVI Publishing Co Inc.
    • (1985) Advances in Meat Research. Electrical Stimulation , vol.1
    • Cross, H.R.1    Seideman, S.C.2
  • 2
    • 84985162754 scopus 로고
    • Relationship of myofibril fragmentation index to certain chemical, physical and sensory characteristics of bovine longissimus muscle
    • Culler, R. D., Parrish, F. C., Smith, G. C., & Cross, H. R. (1978). Relationship of myofibril fragmentation index to certain chemical, physical and sensory characteristics of bovine longissimus muscle. Journal of Food Science, 43, 1177-1180.
    • (1978) Journal of Food Science , vol.43 , pp. 1177-1180
    • Culler, R.D.1    Parrish, F.C.2    Smith, G.C.3    Cross, H.R.4
  • 3
    • 0001383470 scopus 로고
    • Optimisation of tenderisation, ageing and tenderness
    • Dransfield, E. (1994), Optimisation of tenderisation, ageing and tenderness. Meat Science, 36, 105-121.
    • (1994) Meat Science , vol.36 , pp. 105-121
    • Dransfield, E.1
  • 4
    • 58149367740 scopus 로고
    • Cold shortening toughness in excised pork
    • Dransfield, E., & Lockyer, D. K. (1985). Cold shortening toughness in excised pork. Meat Science, 13, 19-32.
    • (1985) Meat Science , vol.13 , pp. 19-32
    • Dransfield, E.1    Lockyer, D.K.2
  • 5
    • 0009360912 scopus 로고
    • Post mortem conditioning of meat
    • A. M. Pearson, & T. R. Dutson (Eds.) Connecticut: AVI Publishing Co Inc.
    • Dutson, T. R., & Pearson, A. M. (1985). Post mortem conditioning of meat. In A. M. Pearson, & T. R. Dutson (Eds.), Advances in meat research. Electrical stimulation Vol. 1 (pp. 45-72). Connecticut: AVI Publishing Co Inc.
    • (1985) Advances in Meat Research. Electrical Stimulation , vol.1 , pp. 45-72
    • Dutson, T.R.1    Pearson, A.M.2
  • 7
    • 0001906486 scopus 로고
    • Conditioning of meat from different species. Relationship between tenderising and levels of cathepsin B, cathepsin L, calpain I and calpain II and β-glucuronidase
    • Etherington, D. J., Taylor, M. A. J., & Dransfield, E. (1987). Conditioning of meat from different species. Relationship between tenderising and levels of cathepsin B, cathepsin L, calpain I and calpain II and β-glucuronidase. Meat Science, 20, 1-18.
    • (1987) Meat Science , vol.20 , pp. 1-18
    • Etherington, D.J.1    Taylor, M.A.J.2    Dransfield, E.3
  • 8
    • 38249013987 scopus 로고
    • Effects of ultrarapid chilling and ageing on length of sarcomeres and tenderness of pork
    • Feldhusen, F., & Kuhne, M. (1992). Effects of ultrarapid chilling and ageing on length of sarcomeres and tenderness of pork. Meat Science, 32, 161-171.
    • (1992) Meat Science , vol.32 , pp. 161-171
    • Feldhusen, F.1    Kuhne, M.2
  • 9
    • 85005731466 scopus 로고
    • The ante-rigor excision and air cooling of beef semimembranosus muscles at temperatures between -5 °C and + 15 °C
    • Follett, M. J., Norman, G. A., & Ratcliff, P. W. (1974). The ante-rigor excision and air cooling of beef semimembranosus muscles at temperatures between -5 °C and + 15 °C. Journal of Food Technology, 9, 509-523.
    • (1974) Journal of Food Technology , vol.9 , pp. 509-523
    • Follett, M.J.1    Norman, G.A.2    Ratcliff, P.W.3
  • 10
    • 0024402489 scopus 로고
    • Factors affecting polyacrylamide gel electrophoresis and electroblotting of high molecular weight myofibrillar proteins
    • Fritz, J., Swartz, D., & Greaser, M. (1989). Factors affecting polyacrylamide gel electrophoresis and electroblotting of high molecular weight myofibrillar proteins. Analytical Biochemistry, 180, 205-210.
    • (1989) Analytical Biochemistry , vol.180 , pp. 205-210
    • Fritz, J.1    Swartz, D.2    Greaser, M.3
  • 11
    • 0024005687 scopus 로고
    • Localisation of paratropomyosin in skeletal muscle myofibrils and its translocation during postmortem storage of muscles
    • Hattori, A., & Takahashi, K. (1988). Localisation of paratropomyosin in skeletal muscle myofibrils and its translocation during postmortem storage of muscles. Journal of Biochemistry, 103, 809-811.
    • (1988) Journal of Biochemistry , vol.103 , pp. 809-811
    • Hattori, A.1    Takahashi, K.2
  • 12
    • 0037936906 scopus 로고
    • Hot boning of pig carcasses: Influences of chilling conditions on meat quality
    • A. Romita, C. Valin, & A. Taylor (Eds.) London: Elsevier Applied Publishers
    • Honikel, K. O. J., & Reagan, J. O. (1987). Hot boning of pig carcasses: Influences of chilling conditions on meat quality. In A. Romita, C. Valin, & A. Taylor (Eds.), Accelerated processing of meat. London: Elsevier Applied Publishers.
    • (1987) Accelerated Processing of Meat
    • Honikel, K.O.J.1    Reagan, J.O.2
  • 13
    • 0001303853 scopus 로고
    • Sarcomere shortening of prerigor muscle and its influence on drip loss
    • Honikel, K. O., Kim, C. J., Hamm, R., & Roncales, P. (1986). Sarcomere shortening of prerigor muscle and its influence on drip loss. Meat Science, 16, 267-282.
    • (1986) Meat Science , vol.16 , pp. 267-282
    • Honikel, K.O.1    Kim, C.J.2    Hamm, R.3    Roncales, P.4
  • 15
    • 21844490014 scopus 로고
    • Tenderisation of pork as affected by degree of cold-induced shortening
    • Iversen, P., Henckel, P., Larsen, L. M., Monllao, S., & Moller, A. J. (1995). Tenderisation of pork as affected by degree of cold-induced shortening. Meat Science, 40, 171-181.
    • (1995) Meat Science , vol.40 , pp. 171-181
    • Iversen, P.1    Henckel, P.2    Larsen, L.M.3    Monllao, S.4    Moller, A.J.5
  • 17
    • 0030528302 scopus 로고    scopus 로고
    • Effects of postmortem temperature and time on the water holding capacity of hot boned turkey breast and thigh muscle
    • Lesink, M. T., Olson, D. G., Lesiak, C. A., & Ahn, D. U. (1996). Effects of postmortem temperature and time on the water holding capacity of hot boned turkey breast and thigh muscle. Meat Science, 43, 51-60.
    • (1996) Meat Science , vol.43 , pp. 51-60
    • Lesink, M.T.1    Olson, D.G.2    Lesiak, C.A.3    Ahn, D.U.4
  • 18
    • 0002216116 scopus 로고
    • Cold-induced toughness of meat
    • A. M. Pearson & T. R. Dutson (Eds.) Connecticut: AVI Publishing Company
    • Locker, R. H. (1985). Cold-induced toughness of meat. In: A. M. Pearson & T. R. Dutson (Eds.), Advances in meat research. Electrical stimulation Vol. I (pp. 1-45). Connecticut: AVI Publishing Company.
    • (1985) Advances in Meat Research. Electrical Stimulation , vol.1 , pp. 1-45
    • Locker, R.H.1
  • 24
    • 84985070008 scopus 로고
    • Effect of high temperature conditioning on subcellular distribution and levels of lysosomal enzymes
    • Moeller, P. W., Fields, P. A., Dutson, T. R., Landmann, W. A., & Carpenter, Z. L. (1976). Effect of high temperature conditioning on subcellular distribution and levels of lysosomal enzymes. Journal of Food Science, 41, 216-217.
    • (1976) Journal of Food Science , vol.41 , pp. 216-217
    • Moeller, P.W.1    Fields, P.A.2    Dutson, T.R.3    Landmann, W.A.4    Carpenter, Z.L.5
  • 25
    • 84987299751 scopus 로고
    • High temperature effects on lysosomal enzyme distribution and fragmentation of bovine muscle
    • Moeller, P. W., Fields, P. A., Dutson, T. R., Landmann, W. A., & Carpenter, Z. L. (1977). High temperature effects on lysosomal enzyme distribution and fragmentation of bovine muscle. Journal of Food Science, 42, 510-512.
    • (1977) Journal of Food Science , vol.42 , pp. 510-512
    • Moeller, P.W.1    Fields, P.A.2    Dutson, T.R.3    Landmann, W.A.4    Carpenter, Z.L.5
  • 26
    • 0001908705 scopus 로고
    • Effects of altered carcass suspension during rigor mortis on tenderness of pork loin
    • Moller, A. J., & Vestergaard, T. (1986). Effects of altered carcass suspension during rigor mortis on tenderness of pork loin. Meat Science, 18, 77-87.
    • (1986) Meat Science , vol.18 , pp. 77-87
    • Moller, A.J.1    Vestergaard, T.2
  • 27
    • 0011451777 scopus 로고
    • Effect of temperature conditioning on toughness in hot boned pork loins with high or low initial pH
    • Moller, A. J., & Vestergaard, T. (1988). Effect of temperature conditioning on toughness in hot boned pork loins with high or low initial pH. 34th International Congress of Meat Science and Technology, 34, 621-622.
    • (1988) 34th International Congress of Meat Science and Technology , vol.34 , pp. 621-622
    • Moller, A.J.1    Vestergaard, T.2
  • 29
    • 0010768779 scopus 로고
    • Physical and biochemical changes occurring in muscle during storage and preservation
    • Academic Press Orlando
    • Pearson, A. M. (1986) Physical and biochemical changes occurring in muscle during storage and preservation. In: Muscle as food. Academic Press Orlando, p 10, 26 and 103-134.
    • (1986) Muscle as Food , pp. 10
    • Pearson, A.M.1
  • 30
    • 0010987696 scopus 로고
    • Skeletal muscle fibre types
    • Academic Press, San Diego
    • Pearson, A. M. and Young, R. B. (1989) Skeletal muscle fibre types. In: Muscle and meat biochemistry. Academic Press, San Diego, p 235-265.
    • (1989) Muscle and Meat Biochemistry , pp. 235-265
    • Pearson, A.M.1    Young, R.B.2
  • 31
    • 0010812281 scopus 로고
    • Quadratic relationship between early postmortem glycolytic rate and beef tenderness
    • Pike, M. M., Ringkob, T. P., Beekman, D. D., Koh, Y. O., & Gerthoffer, W. T. (1993). Quadratic relationship between early postmortem glycolytic rate and beef tenderness. Meat Science, 34, 13-26.
    • (1993) Meat Science , vol.34 , pp. 13-26
    • Pike, M.M.1    Ringkob, T.P.2    Beekman, D.D.3    Koh, Y.O.4    Gerthoffer, W.T.5
  • 34
    • 0036313465 scopus 로고    scopus 로고
    • Tenderness, ageing rate and meat quality of pork in. Longissimus thoracis et Lumborum after accelerated boning. Part II
    • Rees, M. P., Trout, G. R., & Warner, R. D. (2002). Tenderness, ageing rate and meat quality of pork in. Longissimus thoracis et Lumborum after accelerated boning. Part II. Meat Science, 61(2), 215-224.
    • (2002) Meat Science , vol.61 , Issue.2 , pp. 215-224
    • Rees, M.P.1    Trout, G.R.2    Warner, R.D.3
  • 35
    • 84987345028 scopus 로고
    • Comparison of sarcomere length measurement of cooked chicken pectoralis muscle by laser diffraction and oil immersion microscopy
    • Ruddick, J. E., & Richards, J. F. (1975). Comparison of sarcomere length measurement of cooked chicken pectoralis muscle by laser diffraction and oil immersion microscopy. Journal of Food Science, 40, 500-501.
    • (1975) Journal of Food Science , vol.40 , pp. 500-501
    • Ruddick, J.E.1    Richards, J.F.2
  • 37
    • 43949172570 scopus 로고
    • Structural studies of rigor bovine myofibrils using fluorescence microscopy. 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., & Marsh, B. B. (1993). Structural studies of rigor bovine myofibrils using fluorescence microscopy. II. Influence of sarcomere length on the binding of myosin subfragment-1, alpha-actinin and G-actin to rigor myofibrils. Meat Science, 33,157-190.
    • (1993) Meat Science , vol.33 , pp. 157-190
    • Swartz, D.R.1    Greaser, M.L.2    Marsh, B.B.3
  • 38
    • 0023122944 scopus 로고
    • Calcium induced weakening of z disks in postmortem skeletal muscle
    • Takahashi, K., Kim, O. H., & Yano, K. (1987). Calcium induced weakening of z disks in postmortem skeletal muscle. Journal of Biochemistry, 101, 767-775.
    • (1987) Journal of Biochemistry , vol.101 , pp. 767-775
    • Takahashi, K.1    Kim, O.H.2    Yano, K.3
  • 39
    • 0021912232 scopus 로고
    • Paratropomyosin: A new myofibrillar protein that modifies the actin-myosin interaction in post rigor skeletal muscle. I. Preparation and characterisation
    • Takahashi, K., Nakamura, F., Hattori, A., & Yamanoue, M. (1985a). Paratropomyosin: a new myofibrillar protein that modifies the actin-myosin interaction in post rigor skeletal muscle. I. Preparation and characterisation. Journal of Biochemistry, 97, 1043-1052.
    • (1985) Journal of Biochemistry , vol.97 , pp. 1043-1052
    • Takahashi, K.1    Nakamura, F.2    Hattori, A.3    Yamanoue, M.4
  • 40
    • 0021987010 scopus 로고
    • Paratropomyosin: A new myofibrillar protein that modifies the actin-myosin interaction in post rigor skeletal muscle. II. Distinct function from tropomyosin
    • Takahashi, K., Nakamura, F., Hattori, A., & Yamanoue, M. (1985b). Paratropomyosin: a new myofibrillar protein that modifies the actin-myosin interaction in post rigor skeletal muscle. II. Distinct function from tropomyosin. Journal of Biochemistry, 97, 1053-1056.
    • (1985) Journal of Biochemistry , vol.97 , pp. 1053-1056
    • Takahashi, K.1    Nakamura, F.2    Hattori, A.3    Yamanoue, M.4
  • 41
  • 42
    • 0031286893 scopus 로고    scopus 로고
    • Muscle protein changes post mortem in relation to pork quality traits
    • Warner, R. D., Kauffman, R. G., & Greaser, M. L. (1997). Muscle protein changes post mortem in relation to pork quality traits. Meat Science, 45, 339-352.
    • (1997) Meat Science , vol.45 , pp. 339-352
    • Warner, R.D.1    Kauffman, R.G.2    Greaser, M.L.3
  • 43
    • 21144467507 scopus 로고
    • Quality attributes of major porcine muscles: A comparison with the longissimus lumborum
    • Warner, R. D., Kauffman, R. G., & Russell, R. L. (1993). Quality attributes of major porcine muscles: A comparison with the longissimus lumborum. Meat Science, 33, 359-372.
    • (1993) Meat Science , vol.33 , pp. 359-372
    • Warner, R.D.1    Kauffman, R.G.2    Russell, R.L.3
  • 44
    • 84986519237 scopus 로고
    • Cathepsin D and its effects on myofibrillar proteins: A review
    • Zeece, M. G., & Katoh, K. (1989). Cathepsin D and its effects on myofibrillar proteins: a review. Journal of Food Biochemistry, 13, 157-178.
    • (1989) Journal of Food Biochemistry , vol.13 , pp. 157-178
    • Zeece, M.G.1    Katoh, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.