[On the enzymatic breakdown of tripolyphosphate and diphosphate in minced meat. V. Change in the diphosphatase activity of muscle post mortem (author's transl)].
The diphosphatase (DPase) activity of minced bovine muscle decreased during storage of the intact muscle post mortem (p.m.) but there was only little change after development of rigor mortis. The drop in pH p.m. seems to be not the only reason for the decrease in DPase activity. In the postrigor muscle the DPase activity, measured at pH greater than 6, increased during the breakdown of DP. The rise of activity was the slower the longer the muscle was stored. The result of a mathematical regression analysis, developed for the kinetic study of this anomaly in the breakdown of DP, indicates that a certain mechanism of activation of the initially inactive DPase in muscle exists.
[On the enzymatic breakdown of tripolyphosphate and diphosphate in minced meat. V. Change in the diphosphatase activity of muscle post mortem (author's transl)]. The diphosphatase (DPase) activity of minced bovine muscle decreased during storage of the intact muscle post mortem (p.m.) but there was only little change after development of rigor mortis. The drop in pH p.m. seems to be not the only reason for the decrease in DPase activity. In the postrigor muscle the DPase activity, measured at pH greater than 6, increased during the breakdown of DP. The rise of activity was the slower the longer the muscle was stored. The result of a mathematical regression analysis, developed for the kinetic study of this anomaly in the breakdown of DP, indicates that a certain mechanism of activation of the initially inactive DPase in muscle exists.