[On the enzymatic breakdown of tripolyphosphate and diphosphate in comminuted meat. XI. Influence of heating and freezing (author's transl)].
The tripolyphosphatase and diphosphatase activities of comminuted bovine muscle increase with rising temperature until at about 40 degrees C a denaturation of the enzyme proteins occurs. Prae or post rigor frozen bovine muscle, which was stored at -18 degrees C, shows after thawing and mincing the same tripolyphosphatase activity as the non-frozen tissue post rigor. Freezing and thawing under the same conditions cause a reversible inhibition of the  diphosphatase activity of bovine muscle. The reactivation depends on the pH. This inhibition is probably identical with that occurring during storage of beef at -4 degrees C.
[On the enzymatic breakdown of tripolyphosphate and diphosphate in comminuted meat. XI. Influence of heating and freezing (author's transl)]. The tripolyphosphatase and diphosphatase activities of comminuted bovine muscle increase with rising temperature until at about 40 degrees C a denaturation of the enzyme proteins occurs. Prae or post rigor frozen bovine muscle, which was stored at -18 degrees C, shows after thawing and mincing the same tripolyphosphatase activity as the non-frozen tissue post rigor. Freezing and thawing under the same conditions cause a reversible inhibition of the  diphosphatase activity of bovine muscle. The reactivation depends on the pH. This inhibition is probably identical with that occurring during storage of beef at -4 degrees C.