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| Study on the Tripolyphosphatase （TPPase） Property of Bighead Carp （Aristichthys nobilis） Myosin Subfragment-1 | |
| 作者姓名： | GAO Ruichang XUE Changhu YUAN Li ZHANG Yongqin XUE Yong SUN Yan FENG Hui |
| 作者单位： | GAO Ruichang1),2),XUE Changhu1),YUAN Li2),ZHANG Yongqin1),3),XUE Yong1),SUN Yan1),and FENG Hui1)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 |
| 基金项目： | 国家自然科学基金;国家高技术研究发展计划(863计划) |
| 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 |
| 收稿时间： | 18 September 2006 |
| 修稿时间： | 2006-09-18 |
Study on the tripolyphosphatase (TPPase) property of bighead carp (<Emphasis Type="Italic">Aristichthys nobilis</Emphasis>) myosin subfragment-1 |
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| GAO Ruichang XUE Changhu YUAN Li ZHANG Yongqin XUE Yong SUN Yan FENG Hui.Study on the tripolyphosphatase (TPPase) property of bighead carp ( |
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| Authors: | Gao Ruichang Xue Changhu Yuan Li Zhang Yongqin Xue Yong Sun Yan Feng Hui |
| Institution: | 1. College of Food Science and Engineering, Ocean University of China, Qingdao 266003, P. R. China;School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, P. R. China 2. College of Food Science and Engineering, Ocean University of China, Qingdao 266003, P. R. China 3. School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, P. R. China 4. College of Food Science and Engineering, Ocean University of China, Qingdao 266003, P. R. China;Department of Biological and Pharmaceutical Engineering, Qingdao University of Science and Technology,Qingdao 266042, P. R. China |
| Abstract: | Myosin subfragment-1 was prepared from the myofibrils of bighead carp (Aristichthys nobilis). The myosin subfragment-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°C 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 K M of 3.2mmolL−1. |
| Keywords: | myosin subfragment-1 tripolyphosphatase (TPPase) bighead carp Aristichthys nobilis |
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