J. Anim Sci.
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Journal of Animal Science, Vol 74, Issue 12 2943-2947, Copyright © 1996 by American Society of Animal Science

JOURNAL ARTICLE

Collagen crosslinks in longissimus muscle from lambs expressing the callipyge gene

R. A. Field, R. J. McCormick, D. R. Brown, F. C. Hinds and G. D. Snowder
Department of Animal Science, University of Wyoming, Laramie 82071, USA.

The objective of this study was to determine whether increased amounts of collagen and (or) hydroxylysylpyridinoline crosslinks in longissimus muscle are partially responsible for decreased tenderness when callipyge lambs are compared to normal lambs. The longissimus muscle was used because we believe tenderness is a greater problem in loin chops of callipyge lambs than it is in other cuts. Ten normal and 10 half-sibling lambs expressing the callipyge gene were compared. Lambs were slaughtered at approximately 8 mo of age when they reached a target weight of 59 kg. Dressing percentages were higher for the leaner callipyge lambs that exhibited larger longissimus muscle areas and heavier leg weights (P < .01). Warner-Bratzler shear values for longissimus muscle from callipyge lambs were higher (P < .01) than those from normal lambs. The higher shear values were not explained by amount of muscle collagen or by hydroxylysylpyridinoline crosslink concentration because both collagen percentage (P < .09) and crosslink concentration (P < .04) were lower in callipyge lambs. Therefore, attempts to modify shear values and make loin chops from callipyge lambs more acceptable to consumers should focus on the myofibrillar fraction of muscle.


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C. R. Kerth, S. P. Jackson, C. B. Ramsey, and M. F. Miller
Characterization and consumer acceptance of three muscles from Hampshire x Rambouillet cross sheep expressing the callipyge phenotype
J Anim Sci, September 1, 2003; 81(9): 2213 - 2218.
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Copyright © 1996 by the American Society of Animal Science.