[On the enzymatic breakdown of tripolyphosphate and diphosphate in comminuted meat. X. Influence of substrate concentration (author's transl)].
The tripolyphosphatase activity of comminuted bovine muscle increased with rising substrate concentration (up to 0.8% tripolyphosphate in presence of 2% NaCl). Addition of NaCl increased the maximum velocity (Vmax) of the enzymatic hydrolysis, determined by Lineweaver-Burk plots. From the results it is concluded that the product-dissociation is the rate-limiting step in the breakdown of tripolyphosphate. Increasing diphosphate concentrations caused only a small increase in the diphosphatase activity of minced tissue. Addition of NaCl lowered the Vmax of the diphosphatase reaction.
D000818:Animals; D002417:Cattle; D007700:Kinetics; D008460:Meat / Q000032:analysis*; D009132:Muscles / Q000201:enzymology*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D012964:Sodium / Q000494:pharmacology; D013329:Structure-Activity Relationship
D012964:Sodium; D010744:Phosphoric Monoester Hydrolases
Uber den enzymatischen Abbau von Tripolyphosphat und Diphosphat in zerkleinertem Fleisch. X. Einfluss der Substratkonzentration.