Abstract
Samples of the longissimus muscle from six steers were held at either 37° (HT) or 2° (C) for 12 and 24 hr to study the effect of conditioning temperature and incubation time on collagen properties. More of each collagen component (α₁, α₂, β ₁₁, β ₁₂) was present on SDS gels of collagen solubility did not increase to a great extent in the HT conditioned samples when compared to C samples, the HT treatment increased the postmortem effect. Each collagen component, expressed as a percent of total collagen, remained relatively constant when comparing different temperatures or postmortem times. This indicated that the increase in the concentration of collagen components being absorbed on the gels of 24 hr postmortem samples is mainly caused by the release of more total collagen from the connective tissue matrix, and not by a specific release of any one component. It was also found that some breakage of crosslinks occurred during high temperature conditioning. No change in type III collagen of intramuscular connective tissue was found in this study. To determine the effect of postmortem time and temperature on the release of lysosomal enzymes and changes in connective tissue components, semimembranosus muscles from nine steers were restrained and held at 2° (C) for 60 hours and five portions of each muscle were elevated to 37° (HT) for different 12-hour sequences for the 60 hours. It was observed that the rate of pH decline was more rapid in HT conditioned muscle..
Wu, Jiann-Jiu (1978). Characteristics of bovine intramuscular collagen under various postmortem conditions. Texas A&M University. Texas A&M University. Libraries. Available electronically from
https : / /hdl .handle .net /1969 .1 /DISSERTATIONS -277456.