Changes in ATPase activity and solubility of carp [Cyprinus carpio] myofibrils during frozen storage under three different buffer conditions
1996
Ueda, N. (Hokkaido Univ., Hakodate (Japan). Faculty of Fisheries) | Kosugi, T. | Kitazawa, H. | Inoue, N. | Shinano, H.
The effects of storage temperature (at -4, -11, and -26 degrees C) and buffer concentration (5 and 50 mM) on the solubility and ATPase activity of carp myofibrils were compared among three different kinds of buffer. Three kinds of buffer solution, Tris-HCl, Tris-maleate, and phosphate, in the absence of additional neutral salts, were used for this experimental system. Changes in the solubility and ATPase activity differed among the three different buffers in the 50 mM concentration. The extent of decrease in solubility and ATPase activity in the 50 mM system was smallest with the Tris-maleate and phosphate buffers, respectively. When the myofibrils were stored with Tris-HCl buffer, both the indices for denaturation markedly decreased within 3 weeks. The decrease in solubility prior to ATPase inactivation in the phosphate buffer was similar to the freeze denaturation pattern reported in fish muscle. In the case of 50 mM Tris-maleate buffer, ATPase activity decreased while still retaining solubility. Observations of storage temperature dependence in both the indices suggest that the storage temperature affects on the mobility of water and the volume of unfrozen solution, and the former relates intensively to the freeze denaturation of myofibrils
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