The role of endogenous proteases in the tenderisation of fast glycolysing muscle

Meat Science

Volumn 47, Issue 3-4, 1997, Pages 187-210

  O'Halloran, G R ^a   Troy, D J ^a   Buckley, D J ^b   Reville, W J ^b  

^a ASHTOWN FOOD RESEARCH CENTRE   (Ireland)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

FRIESIA;

EID: 0031287106     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0309-1740(97)00046-6     Document Type: Article

References (79)

1. Beltran, J. A., Jaime, I., Santolaria, P., Sanudo, C., Alberti, P. and Roncalés, P. (1993) Effect of stress-induced high post mortem ultimate pH on protease activity and sensory properties of beef. Proceedings of the 39th International Congress of Meat Science and Technology Calgary, Canada. S3P04.WP.
2. Bendall, J. R. and Wismer-Pedersen, J. (1962) Some properties of the fibrillar proteins of normal and watery pork muscle. Journal of Food Science 27, 144.
3. Bodwell, C. E., Pearson, A. M., Wismer-Pedersen, J. and Bratzler, L. J. (1966) Post-mortem changes in muscle. II. Chemical and physical changes in pork. Journal of Food Science 31, 1.
4. Calkins, C. R. and Seideman, S. C. (1988) Relationship among calcium-dependent protease, cathepsin B and H, and meat tenderness and the response of muscle to aging. Journal of Animal Science 66, 1186.
5. Chambers, J. J., Reville, W. J. and Zeece, M. G. (1994) Lysosomal integrity in post mortem bovine skeletal muscle. Sci. des Aliments 14, 441.
6. Cross, H. R., West, R. L. and Dutson, T. R. (1980) Comparison of methods for measuring sarcomere length in beef semitendinosus muscle. Meat Science 5, 261.
7. Davey, C. L. and Gilbert, K. V. (1969) Studies in meat tenderness. 7. Changes in the fine structure of meat during aging. Journal of Food Science 34, 69.
8. Dayton, W. R., Lepley, R. A. and Schollmeyer, J. V. (1981) The role of muscle proteolytic enzymes in degradation of the myofibril. Proc. Recip. Meat Conf. 34, 17.
9. Dransfield, E. (1992) Modelling post mortem tenderisation-III: role of calpain I in conditioning. Meat Sci. 31, 85.
10. Dransfield, E. (1995) Control of meat texture at an industrial scale. In Expression of Tissue Proteinases and Regulation of Protein Degradation as Related to Meat Quality, ed. A. Ouali, D. I. Demeyer and F. J. M. Smulders, p. 463. ECCEAMST, Utrecht, The Netherlands.
11. Ducastaing, A., Valin, C., Schollmeyer, J. and Cross, R. (1985) Effects of electrical stimulation on post mortem changes in the activities of two Ca dependent neutral proteinases and their inhibitor in beef muscle. Meat Science 15, 193.
12. Ertbjerg, P. (1996) The potential of lysosomal enzymes on post mortem tenderisation of meat. Ph.D. thesis, The Royal Veterinary and Agricultural University, Copenhagen, Denmark.
13. Ertbjerg, P., Møller, A. J. and Larsen, L. M. (1993) Measurement of cathepsin B and B+L in muscle. Personal communication.
14. Etherington, D. J. (1984) The contribution of proteolytic enzymes to post mortem changes in muscle. Journal of Animal Science 59, 1644.
15. Fischer, C. and Hamm, R. (1980) Biochemical studies on fast glycolysing bovine muscle. Meat Science 4, 41.
16. Fritz, J. D. and Greaser, M. L. (1991) Changes in titin and nebulin in post mortem bovine muscle revealed by gel electrophoresis, Western blotting and immunofluorescence microscopy. Journal of Food Science 56, 607.
17. Geesink, G. H., Ouali, A. and Smulders, F. J. M. (1992) Tenderisation, calpain/calpastatin activities and osmolality of 6 different muscles. Proceedings of the 38th International Congress of Meat Science and Technology Clermont-Ferrand, France.
18. Geesink, G. H., Van Laack, R. L. J. M., Barnier, V. M. H. and Smulders, F. J. M. (1994) Does electrical stimulation affect the speed of ageing or ageing response? Sci. des Aliments 14, 409.
19. Genstat. Numerical Alogorithms Group Ltd. Oxford.
20. Goll, D. E., Otsuka, Y., Nagainis, P. A., Shannon, J. D., Sathe, S. K. and Muguruma, M. (1983) Role of muscle proteinases in maintenance of muscle integrity and mass. Journal of Food Biochem. 17, 137.
21. Goll, D. E., Taylor, R. G., Christiansen, J. A. and Thompson, V. F. (1992) Role of proteinases and protein turnover in muscle growth and meat quality. Proceedings of the 44th Annual Reciprocal Meat Conference, National Livestock and Meat Board Chicago, Ill.
22. Hedrick, H. B., Aberle, E. D., Forrest, J. C., Judge, M. D. and Merkel, R. A. (1994) In Principles of Meat Science, 3rd edn, ed. H. B. Hedrick, E. D. Aberle, J. C. Forrest, M. D. Judge and R. A. Merkel, p. 98. Kendall/Hunt Publishing Co., Iowa.
23. Henderson, D. W., Goll, D. E. and Stromer, M. H. (1970) A comparison of shortening and Z-line degradation in post mortem bovine, porcine and rabbit muscle. The American Journal of Anatomy 128, 117.
24. Ho, C. Y., Stromer, M. H. and Robson, R. M. (1994) Identification of the 30 kDa polypeptide in post mortem skeletal muscle as a degradation product of troponin-T. Biochimie 76, 369.
25. Honikel, K. O. and Kim, C-J. (1986) Causes of the development of PSE pork. Fleischwirtsch 66, 349.
26. Huff-Lonergan, E., Parrish, F. C. and Robson, R. M. (1995a) Effects of post mortem ageing time, animal age and sex on degradation of titin and nebulin in bovine longissimus muscle. Journal of Animal Science 73, 1064.
27. Huff-Lonergan, E., Parrish, F. C. and Robson, R. M. (1995b) Degradation of muscle structural proteins by μ-calpain under conditions simulation post mortem pH, temperature and ionic strength. Proceedings of the 42nd International Congress of Meat Science and Technology San Antonio, Texas.
28. Hwan, S-F and Bandman, E. (1989) Studies of desmin and a-actinin degradation in bovine semitendinosus muscle. Journal of Food Science 54, 1426.
29. Iversen, P., Ertbjerg, P., Larsen, L. M., Monllao, S. and Møller, A. J. (1993) An FPLC method for determination of calpains and calpastatin in porcine m. longissimus dorsi. Biochimie 75, 869.
30. Johnson, M. H., Calkins, C. R., Huffman, R. D., Johnson, D. D. and Hargrove, D. D. (1990) Differences in cathepsin B+L and calcium-dependent protease activities among breed type and their relationship to beef tenderness. Journal of Animal Science 68, 2371.
31. Koohmaraie, M., Schollmeyer, J. E. and Dutson, T. R. (1986) Effect of low-calcium-requiring calcium activated factor on myofibrils under varying pH and temperature conditions. Journal of Food Science 51, 28.
32. 2+-dependent proteases, their inhibitor and myofibril fragmentation. Meat Science 19, 187.
33. Koohmaraie, M., Whipple, G., Kretchmar, D. H., Crouse, J. D. and Mersmann, H. J. (1991) Post mortem proteolysis in longissimus muscle from beef, lamb and pork carcasses. Journal of Animal Science 69, 617.
34. Kretchmar, D. H., Hathaway, M. R., Epley, R. J. and Dayton, W. R. (1990) Alterations in post mortem degradation of myofibrillar proteins in muscle of lambs fed a β-adrenergic agonist. Journal of Animal Science 68, 1760.
35. Lawrie, R. A. (1985) In Meat Science. 4th edn. Pergamon Press, Oxford.
36. Marsh, B. B. (1954) Rigor mortis in beef. Journal of Science of Food and Agriculture 5, 70.
37. Marsh, B. B. (1993) Approaches to manipulate post mortem metabolism and meat quality. Proceedings of the 39th International Congress of Meat Science and Technology Calgary, Canada. Review paper. Session 3.
38. Marsh, B. B., Ringkob, T. P., Russell, R. L., Swartz, D. R. and Pagel, L. A. (1987) Effects of early-post mortem glycolytic rate on beef tenderness. Meat Science 21, 241.
39. Marshall, B. K. and Tatum, J. D. (1991) In Beef Progress Report. Colorado State University, Fort Collins, CO.
40. Martin, A. H., Murray, A. C., Jeremiah, L. E. and Dutson, P. J. (1983) Electrical stimulation and carcass aging effects on beef carcasses in relation to post mortem glycolytic rates. Journal of Animal Science 57, 1456.
41. Matsukura, U., Matsumoto, T., Tashiro, Y., Okitani, A. and Kato, H. (1984) Morphological changes in myofibrils and glycerinated muscle fibres on treatment with cathepsin D and L. International Journal of Biochemistry 16, 957.
42. May, S. G., Dolezal, H. G., Gill, D. R., Ray, F. K. and Buchanan, D. S. (1992) Effects of days fed, carcass geade traits, and subcutaneous fat removal on post mortem muscle characteristics and beef palatability. Journal of Animal Science 70, 444.
43. Mikami, M., Whiting, A. M., Taylor, M. A. J., Mackiewicz, R. A. and Etherington, D. J. (1987) Degradation of myofibrils from rabbit, chicken and beef by cathepsin L and lysosomal lysates. Meat Science 21, 81.
44. Moeller, P. W., Field, P. A., Dutson, T. R., Landmann, W. A. and Carpenter, Z. L. (1977) High temperature effects on lysosomal enzymes distribution and fragmentation of bovine muscle. Journal of Food Science 42, 510.
45. Murachi, T. (1983) Calpain and Calpastatin. Trends in Biochemical Science 8, 167.
46. O'Halloran, G. R., Troy, D. J. and Buckley, D. J. (1997) The relationship between early post mortem pH and the tenderisation of beef muscles. Meat Science 45(2), 239.
47. Ouali, A. (1990) Meat tenderization: possible causes and mechanisms. A review. Journal of Muscle Foods 1, 129.
48. Ouali, A. (1992) Proteolytic and physiological mechanisms involved in meat texture development. Biochimie 74, 251.
49. Ouali, A. and Talmant, A. (1990) Calpains and calpastatin distribution in bovine, porcine, and ovine skeletal muscles. Meat Science 28, 331.
50. Ouali, A., Garrel, N., Obled, A., Deval, C., Valin, C. and Penny, I. F. (1987) Comparative action of cathepsins D, B, H, L and of a new lysosomal cysteine proteinase on rabbit myofibrils. Meat Science 19, 83.
51. Penny, I. F., Etherington, D. J., Reeves, J. L. and Taylor, M. A. J. (1984) The action of cathepsin L and Ca-activated neutral proteases on myofibrillar proteins. Proceedings of the 30th European Meeting of the Meat Research Workers Bristol.
52. Pike, M. M., Rinkbob, T. P., Beekman, D. D., Koh, Y. O. and Gerthoffer, W. T. (1993) Quadratic relationship between early post mortem glycolytic rate and beef tenderness. Meat Science 34, 13.
53. Reville, W. J., Joseph, R. L. and Harrington, M. G. (1971) Structural changes during the post rigor storage of some large beef muscles. Proceedings of the 17th European Meeting of the Meat Research Workers Bristol.
54. Richardson, F. L., Stromer, M. H., Huiatt, T. W. and Robson, R. M. (1981) Immunoelectron and immunofluorescence localization of desmin in mature avian muscles. Eur. Journal of Cell Biology 26, 91.
55. Robson, R. (1995) Myofibrillar and cytoskeletal structures and proteins in mature skeletal muscle cells. In Expression of Tissue Proteinases and Regulation of Protein Degradation as Related to Meat Quality. ed. A. Ouali, D. I. Demeyer and F. J. M. Smulders, p. 267. ECCEAMST, Utrecht, The Netherlands.
56. Robson, R., Huiatt, T. W. and Parrish Jr, F. C. (1991) Biochemical and structural properties of titin, nebulin and intermediate filaments in muscle. Recip. Meat Conf. Proc. 44, 7.
57. Roncalés, P., Geesink, G. H., VanLaack, R. L. J. M., Jaime, I., Beltrán, J. A., Barnier, V. H. M. and Smulders, F. J. M. (1995) Meat tenderisation: enzymatic mechanisms. In Expression of Tissue Proteinases and Regulation of Protein Degradation as Related to Meat Quality, ed. A. Ouali, D. I. Demeyer and F. J. M. Smulders, p. 311. ECCEAMST, Utrecht, The Netherlands.
58. Salm, C. P., Forrest, J. C., Aberle, E. D., Mills, E. W., Snyder, A. C. and Judge, M. D. (1983) Bovine muscle shortening and protein degradation after electrical stimulation, excision and chilling. Meat Science 8, 163.
59. Schreurs, F. J. G., Van Der Heide, D., Leenstra, F. R. and De Wit, W. (1995) Endogenous proteolytic enzymes in chicken muscles. Differences among strains with different growth rates and protein efficiencies. Poultry Science 74, 523.
60. Scopes, R. K. (1964) The influence of post mortem conditions on the solubilities of muscle proteins. Biochem. J. 91, 201.
61. Shackelford, S. D., Koohmaraie, M., Miller, M. F., Crouse, J. D. and Reagan, J. O. (1991) An evaluation of tenderness of the longissimus muscle of Angus by Hereford versus Brahman crossed heifers. Journal of Animal Science 69, 171.
62. Shackelford, S. D., Koohmaraie, M. and Savell, J. W. (1994) Evaluation of longissimus dorsi muscle pH at three hours post mortem as a predictor of beef tenderness. Meat Science 37, 195.
63. Sheridan, J. J. (1990) The ultra-rapid chilling of lamb carcasses. Meat Science 28, 31.
64. Slinde, E. and Kryvi, H. (1986) Z-Disk digestion of isolated bovine myofibrils byan endogenous calcium activated neutral proteinase. Meat Science 16, 45.
65. Smulders, F. J. M., Marsh, B. B., Swartz, D. R., Russell, R. L. and Hoenecke, M. E. (1990) Beef tenderness and sarcomere length. Meat Science 28, 349.
66. Stagni, N. and deBernard, B. (1968) Lysosome enzyme activity in rat and beefskeletal muscle. Biochim. Biophys. Acta 170, 129.
67. 2+-activated protease in stored muscle. Meat Science 7, 269.
68. Suzuki, A., Saito, M. and Nonami, Y. (1985) Localization of Z-nin and 34,000 Dalton protein in isolated Z-disk sheets of rabbit skeletal muscle. Agricultural and Biological Chemistry 49, 537.
69. SYSTAT, Inc. (1990) Evanston, IL.
70. Taylor, R. G., Geesink, G. H., Thompson, V. F., Koohmaraie, M. and Goll, D. E. (1995) Is Z-disk degradation responsible for post mortem tenderisation? Journal of Animal Science 73, 1351.
71. Thompson, V. F., Taylor, R. G., Goll, D. E., Huff, E. J. and Robson, R. M. (1993) Effect of m-and m-calpain on bovine skeletal muscle myofibrils and IZI brushes. Mol. Biol. Cell 4, 386a.
72. Troy, D. (1987) The effect of carcass treatments on the breakdown of myofibrillar proteins during conditioning of beef muscle. M.Sc. thesis, University College Dublin, Ireland.
73. Tsitsilonis, O. E., Vazeou, S., Yialouris, P. P., Vandekerckhove, J., Stoeva, S., Voelter, W. and Troy, D. J. (1996) Identification by sequence analysis of some critical (30 kDa) proteins in aged beef. Meat Focus International, 77.
74. 2+-dependent neutral proteinases and their specific inhibitor during post mortem storage of rabbit skeletal muscle. Journal of Science of Food and Agriculture 34, 1241.
75. Weibel, E. R., Gonzague, S. K. and Scherle, W. F. (1966) Practical stereological methods for morphometric cytology. Journal of Cell Biology 30, 23.
76. Weisman, G. (1964) Labilization and stabilization of lysosomes. Fed. Proc., Fed. Am. Soc. Exp. Biol. 23, 1038.
77. Whipple, G., Koomaraie, M., Dikeman, M. E., Crouse, J. D., Hunt, M. C. and Klemm, R. D. (1990a) Evaluation of attributes that affect longissimus muscle tenderness in bos taurus and bos indicus cattle. Journal of Animal Science 68, 2716.
78. Whipple, G., Koohmaraie, M., Dikeman, M. E. and Crouse, J. D. (1990b) Predicting beef-longissimus tenderness from various biochemical and histological muscle traits. Journal of Animal Science 68, 4193.
79. Wu, F. Y., Dutson, T. R., Valin, C., Cross, H. R. and Smith, S. B. (1985) Aging index, lysosomal enzyme activities, and meat tenderness in muscles from electrically stimulated bull and steer carcasses. Journal of Food Science 50, 1025.