Efecto de la súper refrigeración sobre la textura de la carne de matrinx？ (Brycon cephalus)

to determine the mechanisms that cause the post mortem muscle softness of the matrinx？, the changes were observed immediately after death in the micro structure of the muscle and after 12 hours of storage at -3 °c. observations by transmission electron microscope agree with the results obtained noting the breaking strength in the muscle measured with a texturometer. the values of the breaking strength on the fish muscle were smaller after chilling. at the same time, it was observed that collagen fibers in the pericellular connective tissue had disintegrated. on the other hand, no evident breakdown of z-discs was observed. it is suggested that the post-mortem tenderization of matrinx？ muscle during chilled storage was due to the disintegration of collagen fibers in the pericellular connective tissue, and, to a smaller degree, to the weakening of z-disk.