Assessment of the relationship between chemical components and palatability of major beef muscles and muscle groups

Meat Science

Volumn 65, Issue 3, 2003, Pages 1013-1019

  Jeremiah, L E ^a   Dugan, M E R ^a   Aalhus, J L ^a   Gibson, L L ^a  

^a LACOMBE RESEARCH CENTRE   (Canada)

Author keywords

Beef; Chemical components; Hydroxyproline; Muscle; Palatability attributes

Indexed keywords

FLAVORS; MUSCLE; PROTEINS; TEXTURES;

BEEF MUSCLES;

MEATS;

EID: 0038043584     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0309-1740(02)00309-1     Document Type: Article

References (42)

1. Aalhus, J. L., Price, M. A., Shand, P. J., & Hawrysh, Z. J. (1991). Endurance exercised growing sheep. II Tenderness increase and change in meat quality. Meat Science, 29, 57-68.
2. Avery, N. C., Sims, T. J., Warkup, C., & Bailey, A. J. (1996). Collagen cross-linking in porcine M. longissimus lumborum. Absence of a relationship with variation in texture at pork weight. Meat Science, 42(3), 355-369.
3. Bailey, A. J. (1972). The basis of meat tenderness. Journal of the Science of Food and Agriculture, 23, 995-1007.
4. Bailey, A. J. (1985). The role of collagen in the development of muscle and its relationship to eating quality. Journal of Animal Science, 60(6), 1580-1587.
5. Bailey, A. J., & Sims, T. S. (1977). Meat tenderness: distribution of molecular species of collagen in bovine muscle. Journal of the Science of Food and Agriculture, 28, 565-570.
6. Bendall, J. R. (1967). The elastin content of various muscles of beef animals. Journal of the Science of Food and Agriculture, 18, 553-558.
7. Berry, B. W., Smith, G. C., & Carpenter, Z. L. (1974). Relationships of certain muscle, cartilage, and bone traits to tenderness of beef longissimus. Journal of Food Science, 39(4), 819-824.
8. Burson, D. E., & Hunt, M. C. (1986). Proportion of collagen types I and III in four bovine muscles differing in tenderness. Journal of Food Science, 51(1), 51-53.
9. Burson, D. E., Hunt, M. C., Unruh, J. A., & Dikeman, M. E. (1986). Proportion of type I and III collagen in longissimus collagen from bulls and steers. Journal of Food Science, 63(2), 453-456.
10. Cross, H. R., Carpenter, Z. L., & Smith, G. C. (1973). Effects of intramuscular collagen and elastin on bovine muscle tenderness. Journal of Food Science, 38(6), 998-1003.
11. Cross, H. R., Schaunbacher, B. D., & Crouse, J. D. (1984). Sex, age, and breed related changes in bovine testosterone and intramuscular collagen. Meat Science, 10, 187-195.
12. Crouse, J. D., Cross, H. R., & Seideman, S. C. (1985). Effects of sex condition, genotype, diet and carcass electrical stimulation on the collagen content and palatability of two bovine muscles. Journal of Animal Science, 60(5), 1228-1234.
13. Duance, V. C., Restell, D. J., Beard, H., Bourne, F. J., & Bailey, A. J. (1977). The location of collagen types in skeletal muscle. FEBS Letters, 79, 248-252.
14. Dugan, M. E. R., Thacker, R. D., Aalhus, J. L., Jeremiah, L. E., & Lien, K. A. (2000). Analysis of 4-hydroxyproline using 4-chloro-7-nitrobenzo-2-oxa-1, 3-diazol derivitization and micellar electro-kinetic chromotography combined with laser reduced fluorescence detection. Journal of Chromotography, B., 744, 195-199.
15. Dutson, T. R. (1974). Connective tissue. In: Proceedings of the Meat Industry Research Conference (pp. 99-107), Washington District of Columbia: American Meat Institute Foundation.
16. Field, R. A. (1968). Effect of connective tissue characteristics on tenderness. Journal of Animal Science, 27(4), 1.
17. Field, R. A., Riley, M. L., & Cheng, Y. (1969). Epimysial connective tissue scores as related to beef tenderness. Journal of Food Science, 34(6), 514-518.
18. Flint, T. O., & Pickering, K. (1984). The histochemical estimation of connective tissue in meat and meat products. Journal of the Science of Food and Agriculture, 35, 1263-1264.
19. Hall, J. B., & Hunt, M. C. (1982). Collagen solubility of A-maturity bovine longissimus muscle as affected by nutritional regimen. Journal of Animal Science, 55(2), 321-328.
20. Herring, H. K., Cassens, R. G., & Briskey, E. J. (1967). Factors affecting collagen solubility in bovine muscles. Journal of Food Science, 32, 534-538.
21. Horgan, D. J., Jones, P. N., King, N. L., Kurth, L. B., & Kuypers, R. (1991). The relationship between animal age and the thermal stability and cross-link content of collagen from five goat muscles. Meat Science, 29, 251-262.
22. Jeremiah, L. E. (1978). A review of factors affecting meat quality. Lacombe Research Station Technical Bulletin Number 1, Lacombe, Alberta, Canada.
23. Jeremiah, L. E. (1982). A review of factors influencing selection, consumption, and acceptability of meat purchases. Journal of Consumer Studies and Home Economics, 6, 137-153.
24. Jeremiah, L. E., Carpenter, Z. L., Smith, G. C., & Butler, O. D. (1970). Marbling as an indicator of palatability. Texas Agricultural Experiment Station Departmental Technical Report Number 22, College Station, Texas.
25. Jeremiah, L. E., Dugan, M. E. R., Aalhus, J. L., & Gibson, L. L. (in press). Assessment of the cooking, and chemical properties of the major beef muscles and muscle groups. Meat Science. doi:10.1016/S0309-1740(02)00308-X.
26. Jeremiah, L. E., Gibson, L. L., Aalhus, J. L., & Dugan, M. E. R. (in press). Assessment of palatability attributes of the major beef muscles and muscle groups. Meat Science. doi:10.1016/S0309-1740(02)00307-8.
27. Ledward, D. A. (1984). Thermal stability of connective tissue in meat and meat products. Journal of the Science of Food and Agriculture, 35, 1262.
28. Lewis, G. J., & Purslow, P. P. (1989). The strength and stiffness of perimysial connective tissue isolate from cooked beef muscle. Meat Science, 26, 255-269.
29. Light, N., & Champion, A. E. (1984). Characterization of muscle epimysium and epimysium collagen. Biochemical Journal, 219, 1017-1026.
30. Light, N., Champion, A. E., Voyle, C., & Bailey, A. J. (1985). The role of epimysial, perimysial, and endomysial collagen in determining texture in six bovine muscles. Meat Science, 13, 137-149.
31. Light, N., Voyle, C., & Champion, A. E. (1984). Relationship between collagen content and type and texture of different muscles. Journal of the Science of Food and Agriculture, 35, 1261-1262.
32. Loyd, E. J., & Hiner, R. L. (1959). Relation between hydroxyproline of alkaline-insoluble protein and tenderness of bovine muscle. Journal of Agricultural and Food Chemistry, 7, 860-862.
33. McClain, P. E., Mullins, A. M., Hansard, S. L., Fox, J. D., & Boulware, R. E. (1965). Relationship of alkaline insoluble collagen to tenderness of three bovine muscles. Journal of Animal Science, 24, 1107-1110.
34. McCormick, R. J. (1994). The flexibility of the collagen compartment of muscle. Meat Science, 36, 79-91.
35. Nishimura, T., Hottori, A., & Takahashi, K. (1999). Structural changes in intramascular connective tissue during the fattening of Japanese black cattle. Effect of marbling on beef tenderization. Journal of Animal Science, 77(1), 93-104.
36. Parrish, F. C. Jr, Bailey, M. E., & Naumann, H. D. (1962). Hydroxyproline as a measure of beef tenderness. Food Technology, 16, 68-71.
37. Puri, S. C., & Mullen, K. (1980). Applied statistics for food and agricultural scientists. Boston, Massachusetts: G.K. Hall. Medical Publishers.
38. Ritchey, S. J., & Hosteller, R. L. (1964). Characterization of the eating quality of four beef muscles from animals of different ages, by panel scores, shear force values, extensibility of muscle fibers, and collagen content. Food Technology, 18, 1067-1070.
39. Rowe, R. W. D. (1986). Elastin in bovine semitendinosus and longissimus muscle. Meat Science, 17, 293-312.
40. Segars, R. A., Nordstrom, H. A., & Kapsalis, J. G. (1974). Textural characteristics of beef muscle. Journal of Texture Studies, 8, 283-297.
41. Shimokomaki, M., Elsden, D. F., & Bailey, A. J. (1972). Meat tenderness. Age related changes in bovine intramuscular collagen. Journal of Food Science, 37(6), 892-896.
42. Young, O. A., & Braggins, T. J. (1993). Tenderness of ovine semimembranosus. Is collagen concentration or solubility the critical factor? Meat Science, 35, 213-222.