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Study on the Tripolyphosphatase (TPPase) Property of Bighead Carp (Aristichthys nobilis) Myosin Subfragment-1

查看全文 作　　者：GAO [1,2]Ruichang;XUE [1]Changhu;YUAN [2]Li;ZHANG [1,3]Yongqin;XUE [1]Yong;SUN [1]Yan;FENG [1]Hui 高影响力作者 机构地区：[1]College of Food Science and Engineering, Ocean University of China, Qingdao 266003, P. R. China;[2]School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, P. R. China;[3]Department of Biological and Pharmaceutical Engineering, Qingdao University of Science and Technology, Qingdao 266042, P. R. China高影响力机构 出　　处：《Journal of Ocean University of China》索引2007年第6卷第4期,共5页高影响力期刊 基　　金：This work was supported by the National Natural Science Foundation of China (No. 30671632);supported by the National High-tech Research and Development Project of China (No. 2006AA09Z444). 摘　　要：Myosin subfragment-1 was prepared from the myofibrils of bighead carp (Aristichthys nobilis). The myosin subfrag- ment-1 was proved to have the activity of tripolyphosphatase (TPPase) responding to the hydrolysis of sodium tripolyphosphate (STPP). The optimum temperature and pH for the TPPase of myosin subfragment-1 were 30℃ and pH 5.0, and at pH 8.0 the TPPase also showed a high activity. Mg2+ was necessary to TPPase. The TPPase activity of myosin subfragment-1 was activated by Mg2+ under low concentrations, but was inhibited when the concentration was over 17 mmolL-1. The TPPase activity was also affected by KCl. The optimum concentration of KCl for TPPase was 0.3 molL-1 under the condition of 17 mmolL-1 Mg2+. The TPPase activity was significantly inhibited by EDTA-Na2. Reagents such as KBr, KI and KIO3 could inhibit the TPPase effectively. K2Cr2O7 as well as KMnO7 and KNO3 exhibited weak inhibiting effects. The TPPase converted STPP to pyrophosphate (PP) and orthophosphate (Pi) stoichiometrically with a KM of 3.2 mmolL-1. 关 键 词：肌浆球蛋白亚碎片-1 生物特性 花鲢 胖头鱼 海洋生物
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