中文摘要：

采用离子色谱方法检测添加的焦磷酸四钠（TSPP）在新鲜碎鳙鱼肉中所发生的水解过程，并研究了焦磷酸盐水解酶（PPase）粗酶的特性。研究结果表明，添加到新鲜碎鳙鱼肉中的TSPP能被水解为单磷酸（Pi）；鳙鱼肉中存在PPase，并且是水溶性蛋白。PPase粗酶水解TSPP的最适温度为50℃，最适pH为8．0。Mg^2＋、Mn^2＋和Co^2＋均可以激活PPase，但是Mg^2＋激活酶能力最强。Mg^2＋浓度为1mol·L^-1时，PPase活性达到了0．023μmol·min^-1·mg^-1，显著高于其他两种金属离子的激活作用。葡萄糖-6-磷酸（G-6-P）能够强烈抑制PPase活性；EDTA—Na2在浓度小于1mol·L^-1能激活酶，但浓度大于1mol·L^-1时却能够强烈抑制PPase活性。

英文摘要：

The hydrolysis of sodium pyrophosphate （TSPP） in the fresh Aristichthys nobilis minced meat was studied by using ion chromatography （IC） in this work. The biochemical properties of the crude pyrophosphatase （PPase） were also studied. The results showed that TSPP was hydrolyzed to orthophosphate （Pi） in A. nobilis minced meat. There was a resoluble pyrophosphatase in the A. nobilis meat. The optimum temperature and pH for the crude PPase activity of A. nobilis meat was 50℃, and 8.0, respectively. The PPase activity was activated by Mg^2＋ , Mn^2＋ and Co^2＋, but Mg^2＋ was the more suitbale to the crude PPase. Under the condition of 1 mol.L^-1 Mg^2＋ , the PPase activity was 0. 023 μmol.min^-1.mg^-1. Glucose 6-phosphate （G-6-P） could inhibit the activity of crude PPase. The crude PPase activity was activated under the condition of below 1 mol . L^-1 EDTA-Na2, but was strongly inhibited when the concentration of EDTA-Na2 over 1 mol. L^-1