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Updated: May 27, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
Published on: September 20, 2012
The effects of conditioning on meat collagen: Part 1-Evidence for gross in situ proteolysis
1Food Studies Division, Department of Catering and Hotel Management, Dorset Institute of Higher Education, Poole, Dorset BH12 5BB, UK.
Abstract:
The relative effectiveness of various reagents was investigated to determine the best method for extracting damaged collagen or collagen fragments from conditioned meat. SDS- and urea-washing were showd to yield clean connective tissue preparations and to extract the largest quantities of soluble collagen from perimysial preparations. Neutral 6m urea was used thereafter to extract soluble material from perimysial and endomysial preparations made from unconditioned and conditioned beef muscles. Eight bovine muscles of varying quality were examined. Conditioned muscles yielded significantly greater quantities of solubilized perimysial material than unconditioned muscles (P = 0·096) although the total collagen solubilized was very low (3·2-5·6% of total perimysial collagen). The amount of collagen or collagen fragments extracted from the eight perimysial preparations from conditioned muscles was significantly higher (P = 0·015) than from unconditioned muscles. Considerable variability in the percentage solubility of collagen from conditioned muscle perimysium was seen. This appeared to be site-specific. It was not possible to demonstrate similar changes in endomysial preparations due to the difficulty in quantitating the relatively low amounts of collagen in these fractions.
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