[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.
D004355:Drug Stability; D005615:Freezing; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008460:Meat / Q000032:analysis*; D009132:Muscles / Q000201:enzymology*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D013329:Structure-Activity Relationship
D010744:Phosphoric Monoester Hydrolases
Uber den enzymatischen Abbau von Tripolyphosphat und Diphosphat in zerkleinertem Fleisch. XI. Einfluss des Erhitzens und Gefrierens.