Purification and characterization of myosin-tripolyphosphatase from rabbit Psoas major muscle: Research note

In this study, we investigated the tripolyphosphatase (TPPase) activity responsible for the hydrolysis of tripolyphosphates (TPP) in rabbit Psoas major muscle tissue. After a series of extraction and purification steps, myosin was identified to be a TPPase. Optimum pH and temperature for myosin-TPPase activity were 6.0 and 35 °C, respectively. We also found that myosin-TPPase activity was significantly influenced by Mg2+ and Ca2+ levels, whose optimal concentrations were determined to be 3 and 6 mM, respectively. Furthermore, myosin-TPPase was strongly inhibited by EDTA-4Na+ and KIO3, and was slightly activated by EDTA-2Na+. These results suggest that it may be useful to regulate tripolyphosphate hydrolysis to enhance its function in meat processing.