|
|
||||||||
Meat Research Institute, Langford, Bristol BS18 7DY, U.K.
Abstract
Our identification of a family of genetically distinct collagens specifically distributed in the connective tissue of muscle now poses questions on their possible role in myoblast differentiation, muscle development, turnover and function in the living muscle, and post-rigor in the tenderness of meat. Using collagen-type specific antibodies we have shown temporal transitions in the type of collagen synthesized during myogenesis. Similar temporal transitions are currently being observed during muscle development. Immunofluorescence techniques also indicated that collagen did not play a role in muscle pattern formation. Once the muscle pattern has been established, the specific distribution of the collagen types in the endomysium (IV and V), perimysium (III and I) and epimysium (I) is maintained during growth. Using an arrested growth model we demonstrated that there was no significant loss of the pre-existing collagen, indicating that the mature collagen fibers do not restrict growth. As the growth rate decreased and the animal matures, the collagen fibers, initially stabilized by intermolecular head-to-tail cross-links, form a stable network via multivalent cross-links. These cross-links determine the extent of the tension generated during heating and the residual adhesion between muscle fibers and hence, the greater the proportion present the tougher the meat. It is therefore the quality rather than the quantitiy of the collagen that determines its contribution to the texture of meat.
1 Presented at the symposium on "Red Meat Production and Processing Systems for the 21st Century" at the 75th Annu. Meet, of the Amer. Soc. of Anim. Sci. at Washington State Univ., Pullman, WA, July 2629, 1983.
2 I should like to thank Drs. Light, Shellswell and Duance of the MRI collagen group for their helpful comments during the preparation of this manuscript.
This article has been cited by other articles:
![]() |
S. Vaithiyanathan, B. M. Naveena, M. Muthukumar, P. S. Girish, C. Ramakrishna, A. R. Sen, and Y. Babji Biochemical and Physicochemical Changes in Spent Hen Breast Meat During Postmortem Aging Poult. Sci., January 1, 2008; 87(1): 180 - 186. [Abstract] [Full Text] [PDF] |
||||
![]() |
B. J. Reuter, D. M. Wulf, and R. J. Maddock Mapping intramuscular tenderness variation in four major muscles of the beef round J Anim Sci, October 1, 2002; 80(10): 2594 - 2599. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. N. Sylvestre, D. Balcerzak, C. Feidt, V. E. Baracos, and J. B. Bellut Elevated rate of collagen solubilization and postmortem degradation inmuscles of lambs with high growth rates: Possible relationship with activity of matrix metalloproteinases J Anim Sci, July 1, 2002; 80(7): 1871 - 1878. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |