New recommendations for measuring collagen solubility

LATORRE ME, LIFSCHITZ AL, PURSLOW PP

MEAT SCIENCE

ELSEVIER SCI LTD

Lugar: Amsterdam; Año: 2016 vol. 118 p. 78 - 81

0309-1740

The heat-solubility of intramuscular collagen is usually conducted in 1/4 Ringer´s solution at pH 7.4, despite this ionic strength and pH being inappropriate for post-rigor meat. The current work studied the percentage of soluble collagen and hydrothermal isometric tension characteristics of perimysial strips on bovine semitendinosus muscles in either 1/4 Ringer´s solution, distilled water, PBS, or a solution of the same salt concentration as 1/4 Ringer´s but at pH 5.6. Values of % soluble collagen were lower at pH 7.4 than 5.6. Increasing ionic strength reduced % soluble collagen. The maximum perimysial isometric tension was independent of the bathing medium,but the percent relaxation was higher at pH 7.4 than at pH 5.6, and increased with ionic strength of the media. It is recommended that future measurements of collagen solubility and tests on connective tissue components ofpost-rigor meat should be carried out in a solution of concentrations NaCl and KCl equivalent to those in 1/4 Ringer´s, but at pH 5.6, a pH relevant to post-rigor meat.